1MCZ
BENZOYLFORMATE DECARBOXYLASE FROM PSEUDOMONAS PUTIDA COMPLEXED WITH AN INHIBITOR, R-MANDELATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0009056 | biological_process | catabolic process |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0018924 | biological_process | mandelate metabolic process |
| A | 0019596 | biological_process | mandelate catabolic process |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0009056 | biological_process | catabolic process |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0018924 | biological_process | mandelate metabolic process |
| B | 0019596 | biological_process | mandelate catabolic process |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0009056 | biological_process | catabolic process |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0018924 | biological_process | mandelate metabolic process |
| C | 0019596 | biological_process | mandelate catabolic process |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030976 | molecular_function | thiamine pyrophosphate binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0009056 | biological_process | catabolic process |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0018924 | biological_process | mandelate metabolic process |
| D | 0019596 | biological_process | mandelate catabolic process |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030976 | molecular_function | thiamine pyrophosphate binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0009056 | biological_process | catabolic process |
| E | 0016831 | molecular_function | carboxy-lyase activity |
| E | 0018924 | biological_process | mandelate metabolic process |
| E | 0019596 | biological_process | mandelate catabolic process |
| E | 0019752 | biological_process | carboxylic acid metabolic process |
| E | 0030976 | molecular_function | thiamine pyrophosphate binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0009056 | biological_process | catabolic process |
| F | 0016831 | molecular_function | carboxy-lyase activity |
| F | 0018924 | biological_process | mandelate metabolic process |
| F | 0019596 | biological_process | mandelate catabolic process |
| F | 0019752 | biological_process | carboxylic acid metabolic process |
| F | 0030976 | molecular_function | thiamine pyrophosphate binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0009056 | biological_process | catabolic process |
| G | 0016831 | molecular_function | carboxy-lyase activity |
| G | 0018924 | biological_process | mandelate metabolic process |
| G | 0019596 | biological_process | mandelate catabolic process |
| G | 0019752 | biological_process | carboxylic acid metabolic process |
| G | 0030976 | molecular_function | thiamine pyrophosphate binding |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0009056 | biological_process | catabolic process |
| H | 0016831 | molecular_function | carboxy-lyase activity |
| H | 0018924 | biological_process | mandelate metabolic process |
| H | 0019596 | biological_process | mandelate catabolic process |
| H | 0019752 | biological_process | carboxylic acid metabolic process |
| H | 0030976 | molecular_function | thiamine pyrophosphate binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| I | 0000287 | molecular_function | magnesium ion binding |
| I | 0003824 | molecular_function | catalytic activity |
| I | 0009056 | biological_process | catabolic process |
| I | 0016831 | molecular_function | carboxy-lyase activity |
| I | 0018924 | biological_process | mandelate metabolic process |
| I | 0019596 | biological_process | mandelate catabolic process |
| I | 0019752 | biological_process | carboxylic acid metabolic process |
| I | 0030976 | molecular_function | thiamine pyrophosphate binding |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| J | 0000287 | molecular_function | magnesium ion binding |
| J | 0003824 | molecular_function | catalytic activity |
| J | 0009056 | biological_process | catabolic process |
| J | 0016831 | molecular_function | carboxy-lyase activity |
| J | 0018924 | biological_process | mandelate metabolic process |
| J | 0019596 | biological_process | mandelate catabolic process |
| J | 0019752 | biological_process | carboxylic acid metabolic process |
| J | 0030976 | molecular_function | thiamine pyrophosphate binding |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| K | 0000287 | molecular_function | magnesium ion binding |
| K | 0003824 | molecular_function | catalytic activity |
| K | 0009056 | biological_process | catabolic process |
| K | 0016831 | molecular_function | carboxy-lyase activity |
| K | 0018924 | biological_process | mandelate metabolic process |
| K | 0019596 | biological_process | mandelate catabolic process |
| K | 0019752 | biological_process | carboxylic acid metabolic process |
| K | 0030976 | molecular_function | thiamine pyrophosphate binding |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| L | 0000287 | molecular_function | magnesium ion binding |
| L | 0003824 | molecular_function | catalytic activity |
| L | 0009056 | biological_process | catabolic process |
| L | 0016831 | molecular_function | carboxy-lyase activity |
| L | 0018924 | biological_process | mandelate metabolic process |
| L | 0019596 | biological_process | mandelate catabolic process |
| L | 0019752 | biological_process | carboxylic acid metabolic process |
| L | 0030976 | molecular_function | thiamine pyrophosphate binding |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| M | 0000287 | molecular_function | magnesium ion binding |
| M | 0003824 | molecular_function | catalytic activity |
| M | 0009056 | biological_process | catabolic process |
| M | 0016831 | molecular_function | carboxy-lyase activity |
| M | 0018924 | biological_process | mandelate metabolic process |
| M | 0019596 | biological_process | mandelate catabolic process |
| M | 0019752 | biological_process | carboxylic acid metabolic process |
| M | 0030976 | molecular_function | thiamine pyrophosphate binding |
| M | 0046872 | molecular_function | metal ion binding |
| M | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| N | 0000287 | molecular_function | magnesium ion binding |
| N | 0003824 | molecular_function | catalytic activity |
| N | 0009056 | biological_process | catabolic process |
| N | 0016831 | molecular_function | carboxy-lyase activity |
| N | 0018924 | biological_process | mandelate metabolic process |
| N | 0019596 | biological_process | mandelate catabolic process |
| N | 0019752 | biological_process | carboxylic acid metabolic process |
| N | 0030976 | molecular_function | thiamine pyrophosphate binding |
| N | 0046872 | molecular_function | metal ion binding |
| N | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| O | 0000287 | molecular_function | magnesium ion binding |
| O | 0003824 | molecular_function | catalytic activity |
| O | 0009056 | biological_process | catabolic process |
| O | 0016831 | molecular_function | carboxy-lyase activity |
| O | 0018924 | biological_process | mandelate metabolic process |
| O | 0019596 | biological_process | mandelate catabolic process |
| O | 0019752 | biological_process | carboxylic acid metabolic process |
| O | 0030976 | molecular_function | thiamine pyrophosphate binding |
| O | 0046872 | molecular_function | metal ion binding |
| O | 0050695 | molecular_function | benzoylformate decarboxylase activity |
| P | 0000287 | molecular_function | magnesium ion binding |
| P | 0003824 | molecular_function | catalytic activity |
| P | 0009056 | biological_process | catabolic process |
| P | 0016831 | molecular_function | carboxy-lyase activity |
| P | 0018924 | biological_process | mandelate metabolic process |
| P | 0019596 | biological_process | mandelate catabolic process |
| P | 0019752 | biological_process | carboxylic acid metabolic process |
| P | 0030976 | molecular_function | thiamine pyrophosphate binding |
| P | 0046872 | molecular_function | metal ion binding |
| P | 0050695 | molecular_function | benzoylformate decarboxylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 529 |
| Chain | Residue |
| A | ASP428 |
| A | ASN455 |
| A | THR457 |
| A | TPP533 |
| A | HOH547 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 530 |
| Chain | Residue |
| B | LEU118 |
| B | ARG120 |
| A | ASN117 |
| A | LEU118 |
| A | ARG120 |
| B | ASN117 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 529 |
| Chain | Residue |
| B | ASP428 |
| B | ASN455 |
| B | THR457 |
| B | TPP533 |
| B | HOH551 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 529 |
| Chain | Residue |
| C | ASP428 |
| C | ASN455 |
| C | THR457 |
| C | TPP533 |
| C | HOH550 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 529 |
| Chain | Residue |
| D | ASP428 |
| D | ASN455 |
| D | THR457 |
| D | TPP533 |
| D | HOH553 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 530 |
| Chain | Residue |
| C | ASN117 |
| C | LEU118 |
| C | ARG120 |
| D | ASN117 |
| D | LEU118 |
| D | ARG120 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 529 |
| Chain | Residue |
| E | ASP428 |
| E | ASN455 |
| E | THR457 |
| E | TPP533 |
| E | HOH546 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 530 |
| Chain | Residue |
| E | ASN117 |
| E | LEU118 |
| E | ARG120 |
| F | ASN117 |
| F | LEU118 |
| F | ARG120 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 529 |
| Chain | Residue |
| F | ASP428 |
| F | ASN455 |
| F | THR457 |
| F | TPP533 |
| F | HOH554 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG G 529 |
| Chain | Residue |
| G | ASP428 |
| G | ASN455 |
| G | THR457 |
| G | TPP533 |
| G | HOH550 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG H 529 |
| Chain | Residue |
| H | ASP428 |
| H | ASN455 |
| H | THR457 |
| H | TPP533 |
| H | HOH553 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG H 530 |
| Chain | Residue |
| G | ASN117 |
| G | LEU118 |
| G | ARG120 |
| H | LEU118 |
| H | ARG120 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG I 529 |
| Chain | Residue |
| I | ASP428 |
| I | ASN455 |
| I | THR457 |
| I | TPP533 |
| I | HOH841 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG I 530 |
| Chain | Residue |
| I | ASN117 |
| I | LEU118 |
| I | ARG120 |
| J | ASN117 |
| J | LEU118 |
| J | ARG120 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG J 529 |
| Chain | Residue |
| J | ASP428 |
| J | ASN455 |
| J | THR457 |
| J | TPP533 |
| J | HOH945 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG K 529 |
| Chain | Residue |
| K | ASP428 |
| K | ASN455 |
| K | THR457 |
| K | TPP533 |
| K | HOH549 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG L 529 |
| Chain | Residue |
| L | ASP428 |
| L | ASN455 |
| L | THR457 |
| L | TPP533 |
| L | HOH557 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG L 530 |
| Chain | Residue |
| K | ASN117 |
| K | LEU118 |
| K | ARG120 |
| L | ASN117 |
| L | LEU118 |
| L | ARG120 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG M 529 |
| Chain | Residue |
| M | HOH1255 |
| M | ASP428 |
| M | ASN455 |
| M | THR457 |
| M | TPP533 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG N 529 |
| Chain | Residue |
| N | ASP428 |
| N | ASN455 |
| N | THR457 |
| N | TPP533 |
| N | HOH552 |
| site_id | CC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG N 530 |
| Chain | Residue |
| M | ASN117 |
| N | ASN117 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG O 529 |
| Chain | Residue |
| O | ASP428 |
| O | ASN455 |
| O | THR457 |
| O | TPP533 |
| O | HOH1462 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG P 529 |
| Chain | Residue |
| P | ASP428 |
| P | ASN455 |
| P | THR457 |
| P | TPP533 |
| P | HOH1566 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG P 530 |
| Chain | Residue |
| O | LEU118 |
| P | MET79 |
| P | LEU118 |
| P | PRO119 |
| P | ARG120 |
| site_id | CC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP A 533 |
| Chain | Residue |
| A | GLU375 |
| A | SER376 |
| A | THR377 |
| A | SER378 |
| A | GLY401 |
| A | LEU403 |
| A | GLY427 |
| A | ASP428 |
| A | GLY429 |
| A | SER430 |
| A | TYR433 |
| A | ASN455 |
| A | THR457 |
| A | TYR458 |
| A | GLY459 |
| A | ALA460 |
| A | LEU461 |
| A | MG529 |
| A | RMN534 |
| B | ASN23 |
| B | PRO24 |
| B | GLY25 |
| B | GLU47 |
| B | HIS70 |
| B | ASN77 |
| site_id | CC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE RMN A 534 |
| Chain | Residue |
| A | HIS281 |
| A | THR377 |
| A | GLY401 |
| A | LEU461 |
| A | PHE464 |
| A | TPP533 |
| A | HOH601 |
| B | GLY25 |
| B | SER26 |
| B | HIS70 |
| B | LEU110 |
| site_id | CC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TPP B 533 |
| Chain | Residue |
| A | ASN23 |
| A | PRO24 |
| A | GLY25 |
| A | GLU47 |
| A | HIS70 |
| A | ASN77 |
| B | GLU375 |
| B | SER376 |
| B | THR377 |
| B | SER378 |
| B | GLY401 |
| B | LEU403 |
| B | GLY427 |
| B | ASP428 |
| B | GLY429 |
| B | SER430 |
| B | TYR433 |
| B | ASN455 |
| B | THR457 |
| B | TYR458 |
| B | GLY459 |
| B | ALA460 |
| B | MG529 |
| B | RMN534 |
| site_id | DC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RMN B 534 |
| Chain | Residue |
| A | SER26 |
| A | HIS70 |
| A | LEU110 |
| B | HIS281 |
| B | THR377 |
| B | GLY401 |
| B | LEU461 |
| B | TPP533 |
| B | HOH602 |
| site_id | DC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP C 533 |
| Chain | Residue |
| C | GLU375 |
| C | SER376 |
| C | THR377 |
| C | SER378 |
| C | GLY401 |
| C | LEU403 |
| C | GLY427 |
| C | ASP428 |
| C | GLY429 |
| C | SER430 |
| C | TYR433 |
| C | ASN455 |
| C | THR457 |
| C | TYR458 |
| C | GLY459 |
| C | ALA460 |
| C | LEU461 |
| C | MG529 |
| C | RMN534 |
| D | ASN23 |
| D | PRO24 |
| D | GLY25 |
| D | GLU47 |
| D | HIS70 |
| D | ASN77 |
| site_id | DC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RMN C 534 |
| Chain | Residue |
| C | HIS281 |
| C | THR377 |
| C | GLY401 |
| C | LEU461 |
| C | TPP533 |
| C | HOH603 |
| D | SER26 |
| D | HIS70 |
| D | LEU110 |
| site_id | DC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE TPP D 533 |
| Chain | Residue |
| C | ASN23 |
| C | PRO24 |
| C | GLY25 |
| C | GLU47 |
| C | HIS70 |
| C | ASN77 |
| D | GLU375 |
| D | SER376 |
| D | THR377 |
| D | SER378 |
| D | GLY401 |
| D | LEU403 |
| D | GLY427 |
| D | ASP428 |
| D | GLY429 |
| D | SER430 |
| D | TYR433 |
| D | ASN455 |
| D | THR457 |
| D | TYR458 |
| D | GLY459 |
| D | ALA460 |
| D | LEU461 |
| D | MG529 |
| D | RMN534 |
| D | HOH575 |
| site_id | DC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RMN D 534 |
| Chain | Residue |
| C | SER26 |
| C | HIS70 |
| C | LEU110 |
| D | HIS281 |
| D | THR377 |
| D | GLY401 |
| D | LEU461 |
| D | PHE464 |
| D | TPP533 |
| site_id | DC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP E 533 |
| Chain | Residue |
| E | GLU375 |
| E | SER376 |
| E | THR377 |
| E | SER378 |
| E | GLY401 |
| E | LEU403 |
| E | GLY427 |
| E | ASP428 |
| E | GLY429 |
| E | SER430 |
| E | TYR433 |
| E | ASN455 |
| E | THR457 |
| E | TYR458 |
| E | GLY459 |
| E | ALA460 |
| E | LEU461 |
| E | MG529 |
| E | RMN534 |
| F | ASN23 |
| F | PRO24 |
| F | GLY25 |
| F | GLU47 |
| F | HIS70 |
| F | ASN77 |
| site_id | DC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RMN E 534 |
| Chain | Residue |
| E | HIS281 |
| E | THR377 |
| E | GLY401 |
| E | LEU461 |
| E | TPP533 |
| E | HOH599 |
| F | SER26 |
| F | HIS70 |
| F | LEU110 |
| site_id | DC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP F 533 |
| Chain | Residue |
| E | ASN23 |
| E | PRO24 |
| E | GLY25 |
| E | GLU47 |
| E | HIS70 |
| E | ASN77 |
| F | GLU375 |
| F | SER376 |
| F | THR377 |
| F | SER378 |
| F | GLY401 |
| F | LEU403 |
| F | GLY427 |
| F | ASP428 |
| F | GLY429 |
| F | SER430 |
| F | TYR433 |
| F | ASN455 |
| F | THR457 |
| F | TYR458 |
| F | GLY459 |
| F | ALA460 |
| F | LEU461 |
| F | MG529 |
| F | RMN534 |
| site_id | DC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RMN F 534 |
| Chain | Residue |
| E | SER26 |
| E | HIS70 |
| E | LEU110 |
| F | HIS281 |
| F | THR377 |
| F | GLY401 |
| F | LEU461 |
| F | PHE464 |
| F | TPP533 |
| site_id | EC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP G 533 |
| Chain | Residue |
| G | GLU375 |
| G | SER376 |
| G | THR377 |
| G | SER378 |
| G | GLY401 |
| G | LEU403 |
| G | GLY427 |
| G | ASP428 |
| G | GLY429 |
| G | SER430 |
| G | TYR433 |
| G | ASN455 |
| G | THR457 |
| G | TYR458 |
| G | GLY459 |
| G | ALA460 |
| G | LEU461 |
| G | MG529 |
| G | RMN534 |
| H | ASN23 |
| H | PRO24 |
| H | GLY25 |
| H | GLU47 |
| H | HIS70 |
| H | ASN77 |
| site_id | EC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE RMN G 534 |
| Chain | Residue |
| G | HIS281 |
| G | THR377 |
| G | GLY401 |
| G | LEU461 |
| G | PHE464 |
| G | TPP533 |
| H | GLY25 |
| H | SER26 |
| H | HIS70 |
| H | LEU110 |
| site_id | EC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP H 533 |
| Chain | Residue |
| G | ASN23 |
| G | PRO24 |
| G | GLY25 |
| G | GLU47 |
| G | HIS70 |
| G | ASN77 |
| H | GLU375 |
| H | SER376 |
| H | THR377 |
| H | SER378 |
| H | GLY401 |
| H | LEU403 |
| H | GLY427 |
| H | ASP428 |
| H | GLY429 |
| H | SER430 |
| H | TYR433 |
| H | ASN455 |
| H | THR457 |
| H | TYR458 |
| H | GLY459 |
| H | ALA460 |
| H | MG529 |
| H | RMN534 |
| H | HOH553 |
| site_id | EC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE RMN H 534 |
| Chain | Residue |
| G | SER26 |
| G | HIS70 |
| G | LEU110 |
| H | HIS281 |
| H | THR377 |
| H | GLY401 |
| H | LEU461 |
| H | TPP533 |
| site_id | EC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP I 533 |
| Chain | Residue |
| I | GLU375 |
| I | SER376 |
| I | THR377 |
| I | SER378 |
| I | GLY401 |
| I | LEU403 |
| I | GLY427 |
| I | ASP428 |
| I | GLY429 |
| I | SER430 |
| I | TYR433 |
| I | ASN455 |
| I | THR457 |
| I | TYR458 |
| I | GLY459 |
| I | ALA460 |
| I | MG529 |
| I | RMN534 |
| I | HOH865 |
| J | ASN23 |
| J | PRO24 |
| J | GLY25 |
| J | GLU47 |
| J | HIS70 |
| J | ASN77 |
| site_id | EC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RMN I 534 |
| Chain | Residue |
| I | HIS281 |
| I | THR377 |
| I | GLY401 |
| I | LEU461 |
| I | TPP533 |
| I | HOH899 |
| J | SER26 |
| J | HIS70 |
| J | LEU110 |
| site_id | EC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP J 533 |
| Chain | Residue |
| I | ASN23 |
| I | PRO24 |
| I | GLY25 |
| I | GLU47 |
| I | HIS70 |
| I | ASN77 |
| J | GLU375 |
| J | SER376 |
| J | THR377 |
| J | SER378 |
| J | GLY401 |
| J | LEU403 |
| J | GLY427 |
| J | ASP428 |
| J | GLY429 |
| J | SER430 |
| J | TYR433 |
| J | ASN455 |
| J | THR457 |
| J | TYR458 |
| J | GLY459 |
| J | ALA460 |
| J | LEU461 |
| J | MG529 |
| J | RMN534 |
| site_id | EC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE RMN J 534 |
| Chain | Residue |
| I | SER26 |
| I | HIS70 |
| I | LEU110 |
| J | HIS281 |
| J | THR377 |
| J | GLY401 |
| J | LEU461 |
| J | PHE464 |
| J | TPP533 |
| J | HOH1002 |
| site_id | EC9 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE TPP K 533 |
| Chain | Residue |
| K | GLU375 |
| K | SER376 |
| K | THR377 |
| K | SER378 |
| K | GLY401 |
| K | LEU403 |
| K | GLY427 |
| K | ASP428 |
| K | GLY429 |
| K | SER430 |
| K | TYR433 |
| K | ASN455 |
| K | THR457 |
| K | TYR458 |
| K | GLY459 |
| K | ALA460 |
| K | LEU461 |
| K | MG529 |
| K | RMN534 |
| K | HOH549 |
| K | HOH572 |
| L | ASN23 |
| L | PRO24 |
| L | GLY25 |
| L | GLU47 |
| L | HIS70 |
| L | ASN77 |
| site_id | FC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RMN K 534 |
| Chain | Residue |
| K | HIS281 |
| K | THR377 |
| K | GLY401 |
| K | LEU461 |
| K | PHE464 |
| K | TPP533 |
| L | SER26 |
| L | HIS70 |
| L | LEU110 |
| site_id | FC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TPP L 533 |
| Chain | Residue |
| K | ASN23 |
| K | PRO24 |
| K | GLY25 |
| K | GLU47 |
| K | HIS70 |
| K | ASN77 |
| L | GLU375 |
| L | SER376 |
| L | THR377 |
| L | SER378 |
| L | GLY401 |
| L | LEU403 |
| L | GLY427 |
| L | ASP428 |
| L | GLY429 |
| L | SER430 |
| L | TYR433 |
| L | ASN455 |
| L | THR457 |
| L | TYR458 |
| L | GLY459 |
| L | ALA460 |
| L | MG529 |
| L | RMN534 |
| site_id | FC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RMN L 534 |
| Chain | Residue |
| K | SER26 |
| K | HIS70 |
| K | LEU110 |
| L | HIS281 |
| L | THR377 |
| L | GLY401 |
| L | LEU461 |
| L | TPP533 |
| L | HOH610 |
| site_id | FC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP M 533 |
| Chain | Residue |
| M | GLU375 |
| M | SER376 |
| M | THR377 |
| M | SER378 |
| M | GLY401 |
| M | LEU403 |
| M | GLY427 |
| M | ASP428 |
| M | GLY429 |
| M | SER430 |
| M | TYR433 |
| M | ASN455 |
| M | THR457 |
| M | TYR458 |
| M | GLY459 |
| M | ALA460 |
| M | MG529 |
| M | RMN534 |
| M | HOH1279 |
| N | ASN23 |
| N | PRO24 |
| N | GLY25 |
| N | GLU47 |
| N | HIS70 |
| N | ASN77 |
| site_id | FC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE RMN M 534 |
| Chain | Residue |
| M | HIS281 |
| M | THR377 |
| M | GLY401 |
| M | LEU461 |
| M | TPP533 |
| N | SER26 |
| N | HIS70 |
| N | LEU110 |
| site_id | FC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP N 533 |
| Chain | Residue |
| M | ASN23 |
| M | PRO24 |
| M | GLY25 |
| M | GLU47 |
| M | HIS70 |
| M | ASN77 |
| N | GLU375 |
| N | SER376 |
| N | THR377 |
| N | SER378 |
| N | GLY401 |
| N | LEU403 |
| N | GLY427 |
| N | ASP428 |
| N | GLY429 |
| N | SER430 |
| N | TYR433 |
| N | ASN455 |
| N | THR457 |
| N | TYR458 |
| N | GLY459 |
| N | ALA460 |
| N | MG529 |
| N | RMN534 |
| N | HOH574 |
| site_id | FC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RMN N 534 |
| Chain | Residue |
| M | SER26 |
| M | HIS70 |
| M | LEU110 |
| N | HIS281 |
| N | THR377 |
| N | GLY401 |
| N | LEU461 |
| N | PHE464 |
| N | TPP533 |
| site_id | FC8 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE TPP O 533 |
| Chain | Residue |
| O | GLU375 |
| O | SER376 |
| O | THR377 |
| O | SER378 |
| O | GLY401 |
| O | LEU403 |
| O | GLY427 |
| O | ASP428 |
| O | GLY429 |
| O | SER430 |
| O | TYR433 |
| O | ASN455 |
| O | THR457 |
| O | TYR458 |
| O | GLY459 |
| O | ALA460 |
| O | LEU461 |
| O | MG529 |
| O | RMN534 |
| O | HOH1486 |
| P | ASN23 |
| P | PRO24 |
| P | GLY25 |
| P | GLU47 |
| P | HIS70 |
| P | ASN77 |
| site_id | FC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE RMN O 534 |
| Chain | Residue |
| O | HIS281 |
| O | THR377 |
| O | GLY401 |
| O | LEU461 |
| O | TPP533 |
| P | SER26 |
| P | HIS70 |
| P | LEU110 |
| site_id | GC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE TPP P 533 |
| Chain | Residue |
| O | ASN23 |
| O | PRO24 |
| O | GLY25 |
| O | GLU47 |
| O | HIS70 |
| O | ASN77 |
| P | GLU375 |
| P | SER376 |
| P | THR377 |
| P | SER378 |
| P | GLY401 |
| P | LEU403 |
| P | GLY427 |
| P | ASP428 |
| P | GLY429 |
| P | SER430 |
| P | TYR433 |
| P | ASN455 |
| P | THR457 |
| P | TYR458 |
| P | GLY459 |
| P | ALA460 |
| P | LEU461 |
| P | MG529 |
| P | RMN534 |
| P | HOH1590 |
| site_id | GC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE RMN P 534 |
| Chain | Residue |
| O | SER26 |
| O | HIS70 |
| O | LEU110 |
| P | HIS281 |
| P | THR377 |
| P | GLY401 |
| P | LEU461 |
| P | TPP533 |
Functional Information from PROSITE/UniProt
| site_id | PS00187 |
| Number of Residues | 20 |
| Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGvqlaePerqvIaViGDGS |
| Chain | Residue | Details |
| A | ILE411-SER430 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 96 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN117 | |
| B | ASP428 | |
| B | ASN455 | |
| B | THR457 | |
| C | ASN117 | |
| C | LEU118 | |
| C | ARG120 | |
| C | ASP428 | |
| C | ASN455 | |
| C | THR457 | |
| D | ASN117 | |
| A | LEU118 | |
| D | LEU118 | |
| D | ARG120 | |
| D | ASP428 | |
| D | ASN455 | |
| D | THR457 | |
| E | ASN117 | |
| E | LEU118 | |
| E | ARG120 | |
| E | ASP428 | |
| E | ASN455 | |
| A | ARG120 | |
| E | THR457 | |
| F | ASN117 | |
| F | LEU118 | |
| F | ARG120 | |
| F | ASP428 | |
| F | ASN455 | |
| F | THR457 | |
| G | ASN117 | |
| G | LEU118 | |
| G | ARG120 | |
| A | ASP428 | |
| G | ASP428 | |
| G | ASN455 | |
| G | THR457 | |
| H | ASN117 | |
| H | LEU118 | |
| H | ARG120 | |
| H | ASP428 | |
| H | ASN455 | |
| H | THR457 | |
| I | ASN117 | |
| A | ASN455 | |
| I | LEU118 | |
| I | ARG120 | |
| I | ASP428 | |
| I | ASN455 | |
| I | THR457 | |
| J | ASN117 | |
| J | LEU118 | |
| J | ARG120 | |
| J | ASP428 | |
| J | ASN455 | |
| A | THR457 | |
| J | THR457 | |
| K | ASN117 | |
| K | LEU118 | |
| K | ARG120 | |
| K | ASP428 | |
| K | ASN455 | |
| K | THR457 | |
| L | ASN117 | |
| L | LEU118 | |
| L | ARG120 | |
| B | ASN117 | |
| L | ASP428 | |
| L | ASN455 | |
| L | THR457 | |
| M | ASN117 | |
| M | LEU118 | |
| M | ARG120 | |
| M | ASP428 | |
| M | ASN455 | |
| M | THR457 | |
| N | ASN117 | |
| B | LEU118 | |
| N | LEU118 | |
| N | ARG120 | |
| N | ASP428 | |
| N | ASN455 | |
| N | THR457 | |
| O | ASN117 | |
| O | LEU118 | |
| O | ARG120 | |
| O | ASP428 | |
| O | ASN455 | |
| B | ARG120 | |
| O | THR457 | |
| P | ASN117 | |
| P | LEU118 | |
| P | ARG120 | |
| P | ASP428 | |
| P | ASN455 | |
| P | THR457 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| A | GLU28 | |
| A | HIS281 | |
| A | HIS70 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| J | GLU28 | |
| J | HIS281 | |
| J | HIS70 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| K | GLU28 | |
| K | HIS281 | |
| K | HIS70 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| L | GLU28 | |
| L | HIS281 | |
| L | HIS70 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| M | GLU28 | |
| M | HIS281 | |
| M | HIS70 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| N | GLU28 | |
| N | HIS281 | |
| N | HIS70 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| O | GLU28 | |
| O | HIS281 | |
| O | HIS70 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| P | GLU28 | |
| P | HIS281 | |
| P | HIS70 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| B | GLU28 | |
| B | HIS281 | |
| B | HIS70 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| C | GLU28 | |
| C | HIS281 | |
| C | HIS70 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| D | GLU28 | |
| D | HIS281 | |
| D | HIS70 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| E | GLU28 | |
| E | HIS281 | |
| E | HIS70 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| F | GLU28 | |
| F | HIS281 | |
| F | HIS70 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| G | GLU28 | |
| G | HIS281 | |
| G | HIS70 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| H | GLU28 | |
| H | HIS281 | |
| H | HIS70 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bfd |
| Chain | Residue | Details |
| I | GLU28 | |
| I | HIS281 | |
| I | HIS70 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| A | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| A | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA10 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| J | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| J | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| J | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| J | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| J | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| J | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| J | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA11 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| K | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| K | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| K | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| K | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| K | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| K | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| K | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA12 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| L | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| L | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| L | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| L | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| L | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| L | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| L | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA13 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| M | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| M | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| M | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| M | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| M | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| M | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| M | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA14 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| N | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| N | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| N | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| N | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| N | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| N | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| N | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA15 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| O | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| O | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| O | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| O | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| O | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| O | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| O | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA16 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| P | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| P | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| P | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| P | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| P | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| P | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| P | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| B | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| B | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| C | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| C | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| C | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| C | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA4 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| D | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| D | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| D | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| D | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA5 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| E | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| E | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| E | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| E | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA6 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| F | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| F | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| F | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| F | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA7 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| G | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| G | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| G | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| G | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| G | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| G | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| G | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA8 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| H | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| H | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| H | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| H | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| H | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| H | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| H | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA9 |
| Number of Residues | 7 |
| Details | M-CSA 220 |
| Chain | Residue | Details |
| I | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| I | SER26 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| I | GLU28 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| I | GLU47 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| I | HIS70 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| I | HIS281 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| I | GLY401 | electrostatic stabiliser, hydrogen bond acceptor |
