1RBL
STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0009853 | biological_process | photorespiration |
| A | 0015977 | biological_process | carbon fixation |
| A | 0015979 | biological_process | photosynthesis |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| A | 0019253 | biological_process | reductive pentose-phosphate cycle |
| A | 0031470 | cellular_component | carboxysome |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0009853 | biological_process | photorespiration |
| B | 0015977 | biological_process | carbon fixation |
| B | 0015979 | biological_process | photosynthesis |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| B | 0019253 | biological_process | reductive pentose-phosphate cycle |
| B | 0031470 | cellular_component | carboxysome |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0009853 | biological_process | photorespiration |
| C | 0015977 | biological_process | carbon fixation |
| C | 0015979 | biological_process | photosynthesis |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| C | 0019253 | biological_process | reductive pentose-phosphate cycle |
| C | 0031470 | cellular_component | carboxysome |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0009853 | biological_process | photorespiration |
| D | 0015977 | biological_process | carbon fixation |
| D | 0015979 | biological_process | photosynthesis |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| D | 0019253 | biological_process | reductive pentose-phosphate cycle |
| D | 0031470 | cellular_component | carboxysome |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0009853 | biological_process | photorespiration |
| E | 0015977 | biological_process | carbon fixation |
| E | 0015979 | biological_process | photosynthesis |
| E | 0016829 | molecular_function | lyase activity |
| E | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| E | 0019253 | biological_process | reductive pentose-phosphate cycle |
| E | 0031470 | cellular_component | carboxysome |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0004497 | molecular_function | monooxygenase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0009853 | biological_process | photorespiration |
| F | 0015977 | biological_process | carbon fixation |
| F | 0015979 | biological_process | photosynthesis |
| F | 0016829 | molecular_function | lyase activity |
| F | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| F | 0019253 | biological_process | reductive pentose-phosphate cycle |
| F | 0031470 | cellular_component | carboxysome |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0004497 | molecular_function | monooxygenase activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0009853 | biological_process | photorespiration |
| G | 0015977 | biological_process | carbon fixation |
| G | 0015979 | biological_process | photosynthesis |
| G | 0016829 | molecular_function | lyase activity |
| G | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| G | 0019253 | biological_process | reductive pentose-phosphate cycle |
| G | 0031470 | cellular_component | carboxysome |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0004497 | molecular_function | monooxygenase activity |
| H | 0005515 | molecular_function | protein binding |
| H | 0009853 | biological_process | photorespiration |
| H | 0015977 | biological_process | carbon fixation |
| H | 0015979 | biological_process | photosynthesis |
| H | 0016829 | molecular_function | lyase activity |
| H | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| H | 0019253 | biological_process | reductive pentose-phosphate cycle |
| H | 0031470 | cellular_component | carboxysome |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0009853 | biological_process | photorespiration |
| I | 0015977 | biological_process | carbon fixation |
| I | 0015979 | biological_process | photosynthesis |
| I | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| I | 0019253 | biological_process | reductive pentose-phosphate cycle |
| I | 0031470 | cellular_component | carboxysome |
| J | 0009853 | biological_process | photorespiration |
| J | 0015977 | biological_process | carbon fixation |
| J | 0015979 | biological_process | photosynthesis |
| J | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| J | 0019253 | biological_process | reductive pentose-phosphate cycle |
| J | 0031470 | cellular_component | carboxysome |
| K | 0009853 | biological_process | photorespiration |
| K | 0015977 | biological_process | carbon fixation |
| K | 0015979 | biological_process | photosynthesis |
| K | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| K | 0019253 | biological_process | reductive pentose-phosphate cycle |
| K | 0031470 | cellular_component | carboxysome |
| L | 0009853 | biological_process | photorespiration |
| L | 0015977 | biological_process | carbon fixation |
| L | 0015979 | biological_process | photosynthesis |
| L | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| L | 0019253 | biological_process | reductive pentose-phosphate cycle |
| L | 0031470 | cellular_component | carboxysome |
| M | 0009853 | biological_process | photorespiration |
| M | 0015977 | biological_process | carbon fixation |
| M | 0015979 | biological_process | photosynthesis |
| M | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| M | 0019253 | biological_process | reductive pentose-phosphate cycle |
| M | 0031470 | cellular_component | carboxysome |
| N | 0009853 | biological_process | photorespiration |
| N | 0015977 | biological_process | carbon fixation |
| N | 0015979 | biological_process | photosynthesis |
| N | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| N | 0019253 | biological_process | reductive pentose-phosphate cycle |
| N | 0031470 | cellular_component | carboxysome |
| O | 0009853 | biological_process | photorespiration |
| O | 0015977 | biological_process | carbon fixation |
| O | 0015979 | biological_process | photosynthesis |
| O | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| O | 0019253 | biological_process | reductive pentose-phosphate cycle |
| O | 0031470 | cellular_component | carboxysome |
| P | 0009853 | biological_process | photorespiration |
| P | 0015977 | biological_process | carbon fixation |
| P | 0015979 | biological_process | photosynthesis |
| P | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| P | 0019253 | biological_process | reductive pentose-phosphate cycle |
| P | 0031470 | cellular_component | carboxysome |
Functional Information from PDB Data
| site_id | 1P |
| Number of Residues | 4 |
| Details | THE BINDING SITE OF THE FIRST PHOSPHATE GROUP OF THE CAP |
| Chain | Residue |
| M | PHE65 |
| A | GLY404 |
| A | GLY381 |
| A | GLY403 |
| site_id | 1P2 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| I | PHE65 |
| B | GLY404 |
| B | GLY381 |
| B | GLY403 |
| site_id | 1P3 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| N | PHE65 |
| C | GLY404 |
| C | GLY381 |
| C | GLY403 |
| site_id | 1P4 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| J | PHE65 |
| D | GLY404 |
| D | GLY381 |
| D | GLY403 |
| site_id | 1P5 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| O | PHE65 |
| E | GLY404 |
| E | GLY381 |
| E | GLY403 |
| site_id | 1P6 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| K | PHE65 |
| F | GLY404 |
| F | GLY381 |
| F | GLY403 |
| site_id | 1P7 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| P | PHE65 |
| G | GLY404 |
| G | GLY381 |
| G | GLY403 |
| site_id | 1P8 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| L | PHE65 |
| H | GLY404 |
| H | GLY381 |
| H | GLY403 |
| site_id | 2P |
| Number of Residues | 2 |
| Details | THE BINDING SITE OF THE 2ND PHOSPHATE OF CAP |
| Chain | Residue |
| A | ARG295 |
| A | HIS327 |
| site_id | 2P2 |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| B | ARG295 |
| B | HIS327 |
| site_id | 2P3 |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| C | ARG295 |
| C | HIS327 |
| site_id | 2P4 |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| D | ARG295 |
| D | HIS327 |
| site_id | 2P5 |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| E | ARG295 |
| E | HIS327 |
| site_id | 2P6 |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| F | ARG295 |
| F | HIS327 |
| site_id | 2P7 |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| G | ARG295 |
| G | HIS327 |
| site_id | 2P8 |
| Number of Residues | 2 |
| Details |
| Chain | Residue |
| H | HIS327 |
| H | ARG295 |
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE CAP A 476 |
| Chain | Residue |
| A | THR173 |
| A | LYS175 |
| A | LYS177 |
| A | HIS294 |
| A | ARG295 |
| A | HIS327 |
| A | LYS334 |
| A | LEU335 |
| A | SER379 |
| A | GLY380 |
| A | GLY381 |
| A | GLY403 |
| A | GLY404 |
| B | THR65 |
| B | TRP66 |
| B | ASN123 |
| A | HOH514 |
| A | HOH515 |
| A | HOH520 |
| A | HOH521 |
| A | HOH569 |
| A | HOH570 |
| A | HOH571 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CAP B 476 |
| Chain | Residue |
| A | THR65 |
| A | TRP66 |
| A | ASN123 |
| B | THR173 |
| B | LYS175 |
| B | LYS177 |
| B | HIS294 |
| B | ARG295 |
| B | HIS327 |
| B | LYS334 |
| B | LEU335 |
| B | SER379 |
| B | GLY380 |
| B | GLY381 |
| B | GLY403 |
| B | GLY404 |
| A | HOH502 |
| A | HOH503 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CAP C 476 |
| Chain | Residue |
| C | THR173 |
| C | LYS175 |
| C | LYS177 |
| C | HIS294 |
| C | ARG295 |
| C | HIS327 |
| C | LYS334 |
| C | LEU335 |
| C | SER379 |
| C | GLY380 |
| C | GLY381 |
| C | GLY403 |
| C | GLY404 |
| D | THR65 |
| D | TRP66 |
| D | ASN123 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CAP D 476 |
| Chain | Residue |
| C | THR65 |
| C | TRP66 |
| C | ASN123 |
| D | THR173 |
| D | LYS175 |
| D | LYS177 |
| D | HIS294 |
| D | ARG295 |
| D | HIS327 |
| D | LYS334 |
| D | LEU335 |
| D | SER379 |
| D | GLY380 |
| D | GLY381 |
| D | GLY403 |
| D | GLY404 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CAP H 476 |
| Chain | Residue |
| G | THR65 |
| G | TRP66 |
| G | ASN123 |
| H | THR173 |
| H | LYS175 |
| H | LYS177 |
| H | HIS294 |
| H | ARG295 |
| H | HIS327 |
| H | LYS334 |
| H | LEU335 |
| H | SER379 |
| H | GLY380 |
| H | GLY381 |
| H | GLY403 |
| H | GLY404 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CAP G 476 |
| Chain | Residue |
| G | THR173 |
| G | LYS175 |
| G | LYS177 |
| G | HIS294 |
| G | ARG295 |
| G | HIS327 |
| G | LYS334 |
| G | LEU335 |
| G | SER379 |
| G | GLY380 |
| G | GLY381 |
| G | GLY403 |
| G | GLY404 |
| H | THR65 |
| H | TRP66 |
| H | ASN123 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CAP F 476 |
| Chain | Residue |
| E | THR65 |
| E | TRP66 |
| E | ASN123 |
| F | THR173 |
| F | LYS175 |
| F | LYS177 |
| F | HIS294 |
| F | ARG295 |
| F | HIS327 |
| F | LYS334 |
| F | LEU335 |
| F | SER379 |
| F | GLY380 |
| F | GLY381 |
| F | GLY403 |
| F | GLY404 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CAP E 476 |
| Chain | Residue |
| E | THR173 |
| E | LYS175 |
| E | LYS177 |
| E | HIS294 |
| E | ARG295 |
| E | HIS327 |
| E | LYS334 |
| E | LEU335 |
| E | SER379 |
| E | GLY380 |
| E | GLY381 |
| E | GLY403 |
| E | GLY404 |
| F | THR65 |
| F | TRP66 |
| F | ASN123 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 478 |
| Chain | Residue |
| A | LYS201 |
| A | ASP202 |
| A | ASP203 |
| A | GLU204 |
| A | HIS294 |
| A | HIS327 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT D 478 |
| Chain | Residue |
| D | LYS201 |
| D | ASP202 |
| D | ASP203 |
| D | GLU204 |
| D | HIS294 |
| D | HIS327 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT E 478 |
| Chain | Residue |
| E | LYS201 |
| E | ASP202 |
| E | ASP203 |
| E | GLU204 |
| E | HIS294 |
| E | HIS327 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT F 478 |
| Chain | Residue |
| F | LYS201 |
| F | ASP202 |
| F | ASP203 |
| F | GLU204 |
| F | HIS294 |
| F | HIS327 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT H 478 |
| Chain | Residue |
| H | LYS201 |
| H | ASP202 |
| H | ASP203 |
| H | GLU204 |
| H | HIS294 |
| H | HIS327 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT G 478 |
| Chain | Residue |
| G | LYS201 |
| G | ASP202 |
| G | ASP203 |
| G | GLU204 |
| G | HIS294 |
| G | HIS327 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT C 478 |
| Chain | Residue |
| C | LYS201 |
| C | ASP202 |
| C | ASP203 |
| C | GLU204 |
| C | HIS294 |
| C | HIS327 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B 478 |
| Chain | Residue |
| B | LYS201 |
| B | ASP202 |
| B | ASP203 |
| B | GLU204 |
| B | HIS294 |
| B | HIS327 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 477 |
| Chain | Residue |
| A | ASP203 |
| A | GLU204 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 477 |
| Chain | Residue |
| B | ASP203 |
| B | GLU204 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 477 |
| Chain | Residue |
| C | ASP203 |
| C | GLU204 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 477 |
| Chain | Residue |
| D | ASP203 |
| D | GLU204 |
| site_id | AE3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG E 477 |
| Chain | Residue |
| E | ASP203 |
| E | GLU204 |
| site_id | AE4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG F 477 |
| Chain | Residue |
| F | ASP203 |
| F | GLU204 |
| site_id | AE5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG G 477 |
| Chain | Residue |
| G | ASP203 |
| G | GLU204 |
| site_id | AE6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG H 477 |
| Chain | Residue |
| H | ASP203 |
| H | GLU204 |
| site_id | CA2 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| B | MG477 |
| B | LYS201 |
| B | HIS294 |
| B | SER379 |
| site_id | CA3 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| C | MG477 |
| C | LYS201 |
| C | HIS294 |
| C | SER379 |
| site_id | CA4 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| D | MG477 |
| D | LYS201 |
| D | HIS294 |
| D | SER379 |
| site_id | CA5 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| E | MG477 |
| E | LYS201 |
| E | HIS294 |
| E | SER379 |
| site_id | CA6 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| F | MG477 |
| F | LYS201 |
| F | HIS294 |
| F | SER379 |
| site_id | CA7 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| G | MG477 |
| G | LYS201 |
| G | HIS294 |
| G | SER379 |
| site_id | CA8 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| H | MG477 |
| H | LYS201 |
| H | HIS294 |
| H | SER379 |
| site_id | CAB |
| Number of Residues | 4 |
| Details | OTHER RESIDUES INVOLVED IN BINDING THE CAP |
| Chain | Residue |
| A | MG477 |
| A | LYS201 |
| A | HIS294 |
| A | SER379 |
| site_id | MG |
| Number of Residues | 3 |
| Details | THE MAGNESIUM BINDING SITE |
| Chain | Residue |
| A | LYS201 |
| A | ASP203 |
| A | GLU204 |
| site_id | MG2 |
| Number of Residues | 3 |
| Details |
| Chain | Residue |
| B | LYS201 |
| B | ASP203 |
| B | GLU204 |
| site_id | MG3 |
| Number of Residues | 3 |
| Details |
| Chain | Residue |
| C | LYS201 |
| C | ASP203 |
| C | GLU204 |
| site_id | MG4 |
| Number of Residues | 3 |
| Details |
| Chain | Residue |
| D | LYS201 |
| D | ASP203 |
| D | GLU204 |
| site_id | MG5 |
| Number of Residues | 3 |
| Details |
| Chain | Residue |
| E | LYS201 |
| E | ASP203 |
| E | GLU204 |
| site_id | MG6 |
| Number of Residues | 3 |
| Details |
| Chain | Residue |
| F | LYS201 |
| F | ASP203 |
| F | GLU204 |
| site_id | MG7 |
| Number of Residues | 3 |
| Details |
| Chain | Residue |
| G | LYS201 |
| G | ASP203 |
| G | GLU204 |
| site_id | MG8 |
| Number of Residues | 3 |
| Details |
| Chain | Residue |
| H | LYS201 |
| H | ASP203 |
| H | GLU204 |
Functional Information from PROSITE/UniProt
| site_id | PS00157 |
| Number of Residues | 9 |
| Details | RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE |
| Chain | Residue | Details |
| A | GLY196-GLU204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | LYS175 | |
| E | HIS294 | |
| F | LYS175 | |
| F | HIS294 | |
| G | LYS175 | |
| G | HIS294 | |
| H | LYS175 | |
| H | HIS294 | |
| A | HIS294 | |
| B | LYS175 | |
| B | HIS294 | |
| C | LYS175 | |
| C | HIS294 | |
| D | LYS175 | |
| D | HIS294 | |
| E | LYS175 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: in homodimeric partner |
| Chain | Residue | Details |
| A | ASN123 | |
| B | ASN123 | |
| C | ASN123 | |
| D | ASN123 | |
| E | ASN123 | |
| F | ASN123 | |
| G | ASN123 | |
| H | ASN123 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | THR173 | |
| B | SER379 | |
| C | THR173 | |
| C | LYS177 | |
| C | ARG295 | |
| C | HIS327 | |
| C | SER379 | |
| D | THR173 | |
| D | LYS177 | |
| D | ARG295 | |
| D | HIS327 | |
| A | LYS177 | |
| D | SER379 | |
| E | THR173 | |
| E | LYS177 | |
| E | ARG295 | |
| E | HIS327 | |
| E | SER379 | |
| F | THR173 | |
| F | LYS177 | |
| F | ARG295 | |
| F | HIS327 | |
| A | ARG295 | |
| F | SER379 | |
| G | THR173 | |
| G | LYS177 | |
| G | ARG295 | |
| G | HIS327 | |
| G | SER379 | |
| H | THR173 | |
| H | LYS177 | |
| H | ARG295 | |
| H | HIS327 | |
| A | HIS327 | |
| H | SER379 | |
| A | SER379 | |
| B | THR173 | |
| B | LYS177 | |
| B | ARG295 | |
| B | HIS327 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: via carbamate group => ECO:0000269|PubMed:8245022 |
| Chain | Residue | Details |
| A | LYS201 | |
| B | LYS201 | |
| C | LYS201 | |
| D | LYS201 | |
| E | LYS201 | |
| F | LYS201 | |
| G | LYS201 | |
| H | LYS201 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8245022 |
| Chain | Residue | Details |
| A | ASP203 | |
| E | GLU204 | |
| F | ASP203 | |
| F | GLU204 | |
| G | ASP203 | |
| G | GLU204 | |
| H | ASP203 | |
| H | GLU204 | |
| A | GLU204 | |
| B | ASP203 | |
| B | GLU204 | |
| C | ASP203 | |
| C | GLU204 | |
| D | ASP203 | |
| D | GLU204 | |
| E | ASP203 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | LYS334 | |
| B | LYS334 | |
| C | LYS334 | |
| D | LYS334 | |
| E | LYS334 | |
| F | LYS334 | |
| G | LYS334 | |
| H | LYS334 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:16593333 |
| Chain | Residue | Details |
| A | LYS201 | |
| B | LYS201 | |
| C | LYS201 | |
| D | LYS201 | |
| E | LYS201 | |
| F | LYS201 | |
| G | LYS201 | |
| H | LYS201 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 8245022, 7922027, 8648644 |
| Chain | Residue | Details |
| A | LYS175 | |
| A | LYS201 | |
| A | LYS177 | |
| A | HIS294 | |
| A | ASP203 | |
| A | HIS327 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 8245022, 7922027, 8648644 |
| Chain | Residue | Details |
| B | LYS175 | |
| B | LYS201 | |
| B | LYS177 | |
| B | HIS294 | |
| B | ASP203 | |
| B | HIS327 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 8245022, 7922027, 8648644 |
| Chain | Residue | Details |
| C | LYS175 | |
| C | LYS201 | |
| C | LYS177 | |
| C | HIS294 | |
| C | ASP203 | |
| C | HIS327 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 8245022, 7922027, 8648644 |
| Chain | Residue | Details |
| D | LYS175 | |
| D | LYS201 | |
| D | LYS177 | |
| D | HIS294 | |
| D | ASP203 | |
| D | HIS327 |
| site_id | CSA5 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 8245022, 7922027, 8648644 |
| Chain | Residue | Details |
| E | LYS175 | |
| E | LYS201 | |
| E | LYS177 | |
| E | HIS294 | |
| E | ASP203 | |
| E | HIS327 |
| site_id | CSA6 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 8245022, 7922027, 8648644 |
| Chain | Residue | Details |
| F | LYS175 | |
| F | LYS201 | |
| F | LYS177 | |
| F | HIS294 | |
| F | ASP203 | |
| F | HIS327 |
| site_id | CSA7 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 8245022, 7922027, 8648644 |
| Chain | Residue | Details |
| G | LYS175 | |
| G | LYS201 | |
| G | LYS177 | |
| G | HIS294 | |
| G | ASP203 | |
| G | HIS327 |
| site_id | CSA8 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 8245022, 7922027, 8648644 |
| Chain | Residue | Details |
| H | LYS175 | |
| H | LYS201 | |
| H | LYS177 | |
| H | HIS294 | |
| H | ASP203 | |
| H | HIS327 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| A | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
| A | LYS201 | metal ligand, nucleophile, proton donor |
| A | ASP203 | metal ligand |
| A | GLU204 | metal ligand |
| A | HIS294 | proton acceptor |
| A | LYS334 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| B | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
| B | LYS201 | metal ligand, nucleophile, proton donor |
| B | ASP203 | metal ligand |
| B | GLU204 | metal ligand |
| B | HIS294 | proton acceptor |
| B | LYS334 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| C | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
| C | LYS201 | metal ligand, nucleophile, proton donor |
| C | ASP203 | metal ligand |
| C | GLU204 | metal ligand |
| C | HIS294 | proton acceptor |
| C | LYS334 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| D | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
| D | LYS201 | metal ligand, nucleophile, proton donor |
| D | ASP203 | metal ligand |
| D | GLU204 | metal ligand |
| D | HIS294 | proton acceptor |
| D | LYS334 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| E | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
| E | LYS201 | metal ligand, nucleophile, proton donor |
| E | ASP203 | metal ligand |
| E | GLU204 | metal ligand |
| E | HIS294 | proton acceptor |
| E | LYS334 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| F | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
| F | LYS201 | metal ligand, nucleophile, proton donor |
| F | ASP203 | metal ligand |
| F | GLU204 | metal ligand |
| F | HIS294 | proton acceptor |
| F | LYS334 | electrostatic stabiliser |
| site_id | MCSA7 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| G | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
| G | LYS201 | metal ligand, nucleophile, proton donor |
| G | ASP203 | metal ligand |
| G | GLU204 | metal ligand |
| G | HIS294 | proton acceptor |
| G | LYS334 | electrostatic stabiliser |
| site_id | MCSA8 |
| Number of Residues | 6 |
| Details | M-CSA 907 |
| Chain | Residue | Details |
| H | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
| H | LYS201 | metal ligand, nucleophile, proton donor |
| H | ASP203 | metal ligand |
| H | GLU204 | metal ligand |
| H | HIS294 | proton acceptor |
| H | LYS334 | electrostatic stabiliser |
