2JLA
Crystal structure of E.coli MenD, 2-succinyl-5-enolpyruvyl-6-hydroxy- 3-cyclohexadiene-1-carboxylate synthase - SeMet protein
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0009234 | biological_process | menaquinone biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0030145 | molecular_function | manganese ion binding |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0070204 | molecular_function | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0009234 | biological_process | menaquinone biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0030145 | molecular_function | manganese ion binding |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0070204 | molecular_function | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0009234 | biological_process | menaquinone biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0030145 | molecular_function | manganese ion binding |
C | 0030976 | molecular_function | thiamine pyrophosphate binding |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0070204 | molecular_function | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0009234 | biological_process | menaquinone biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0030145 | molecular_function | manganese ion binding |
D | 0030976 | molecular_function | thiamine pyrophosphate binding |
D | 0042803 | molecular_function | protein homodimerization activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0070204 | molecular_function | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE TPP A 1557 |
Chain | Residue |
A | SER391 |
A | SER444 |
A | ASN469 |
A | GLY471 |
A | GLY472 |
A | GLN473 |
A | ILE474 |
A | MN1558 |
A | HOH2096 |
A | HOH2097 |
A | HOH2098 |
A | LEU392 |
B | PRO30 |
B | GLU55 |
B | THR81 |
B | ALA82 |
A | SER416 |
A | GLY417 |
A | ILE418 |
A | ASP419 |
A | GLY441 |
A | ASP442 |
A | LEU443 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 1558 |
Chain | Residue |
A | ASP442 |
A | ASN469 |
A | GLY471 |
A | TPP1557 |
A | HOH2098 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE TPP B 1557 |
Chain | Residue |
A | PRO30 |
A | GLU55 |
A | THR81 |
A | ALA82 |
B | SER391 |
B | LEU392 |
B | SER416 |
B | GLY417 |
B | ILE418 |
B | ASP419 |
B | GLY441 |
B | ASP442 |
B | LEU443 |
B | SER444 |
B | TYR447 |
B | ASN469 |
B | GLY471 |
B | GLY472 |
B | GLN473 |
B | ILE474 |
B | MN1558 |
B | HOH2099 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 1558 |
Chain | Residue |
B | ASP442 |
B | ASN469 |
B | GLY471 |
B | TPP1557 |
B | HOH2099 |
site_id | AC5 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE TPP C 1557 |
Chain | Residue |
C | SER391 |
C | LEU392 |
C | SER416 |
C | GLY417 |
C | ILE418 |
C | ASP419 |
C | GLY441 |
C | ASP442 |
C | LEU443 |
C | SER444 |
C | ASN469 |
C | GLY471 |
C | GLY472 |
C | GLN473 |
C | ILE474 |
C | MN1558 |
C | HOH2084 |
C | HOH2085 |
C | HOH2086 |
D | PRO30 |
D | GLU55 |
D | THR81 |
D | ALA82 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN C 1558 |
Chain | Residue |
C | ASP442 |
C | ASN469 |
C | GLY471 |
C | TPP1557 |
C | HOH2086 |
site_id | AC7 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE TPP D 1557 |
Chain | Residue |
D | GLY471 |
D | GLY472 |
D | GLN473 |
D | ILE474 |
D | MN1558 |
D | HOH2111 |
C | PRO30 |
C | GLU55 |
C | THR81 |
C | ALA82 |
D | SER391 |
D | LEU392 |
D | SER416 |
D | GLY417 |
D | ILE418 |
D | ASP419 |
D | GLY441 |
D | ASP442 |
D | LEU443 |
D | SER444 |
D | TYR447 |
D | ASN469 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN D 1558 |
Chain | Residue |
D | ASP442 |
D | ASN469 |
D | GLY471 |
D | TPP1557 |
D | HOH2111 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 1559 |
Chain | Residue |
A | SER32 |
A | ARG33 |
A | THR78 |
A | GLN118 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 1559 |
Chain | Residue |
B | SER32 |
B | ARG33 |
B | THR78 |
B | GLN118 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL C 1559 |
Chain | Residue |
C | GLY31 |
C | SER32 |
C | THR78 |
C | GLN118 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL D 1559 |
Chain | Residue |
D | SER32 |
D | THR78 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 1560 |
Chain | Residue |
A | PRO137 |
A | ARG138 |
C | ARG138 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 1560 |
Chain | Residue |
B | ARG138 |
D | ARG138 |
D | HOH2028 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 1560 |
Chain | Residue |
A | ASN390 |
A | SER391 |
A | ARG395 |
A | ARG413 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 1561 |
Chain | Residue |
B | ASN390 |
B | SER391 |
B | ARG395 |
B | ARG413 |
site_id | BC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 1561 |
Chain | Residue |
C | SER391 |
C | ARG395 |
C | ARG413 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL D 1560 |
Chain | Residue |
D | SER391 |
D | ARG395 |
D | ARG413 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MN C 1562 |
Chain | Residue |
C | HIS509 |
C | ASP523 |
C | HOH2087 |
site_id | CC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 1561 |
Chain | Residue |
A | GLU505 |
D | HIS496 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 1562 |
Chain | Residue |
B | LEU506 |
B | LYS507 |
B | THR530 |
B | HOH2095 |
site_id | CC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL D 1561 |
Chain | Residue |
B | THR243 |
D | THR243 |