4R7U
Structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Vibrio cholerae in complex with substrate UDP-N-acetylglucosamine and the drug fosfomycin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| C | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| C | 0051301 | biological_process | cell division |
| C | 0071555 | biological_process | cell wall organization |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008360 | biological_process | regulation of cell shape |
| D | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| D | 0009252 | biological_process | peptidoglycan biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| D | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| D | 0051301 | biological_process | cell division |
| D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 A 501 |
| Chain | Residue |
| A | CYS82 |
| A | GLN109 |
| A | ASP141 |
| A | LYS145 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FFQ A 502 |
| Chain | Residue |
| A | HOH665 |
| A | HOH666 |
| A | HOH667 |
| A | THR90 |
| A | MET91 |
| A | ARG92 |
| A | CYS116 |
| A | ARG398 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UD1 A 503 |
| Chain | Residue |
| A | ASN24 |
| A | TRP96 |
| A | ARG121 |
| A | PRO122 |
| A | VAL123 |
| A | ASP124 |
| A | LEU125 |
| A | LYS161 |
| A | SER163 |
| A | VAL164 |
| A | GLY165 |
| A | ASP306 |
| A | ILE328 |
| A | HOH615 |
| A | HOH617 |
| A | HOH622 |
| A | HOH640 |
| A | HOH657 |
| A | HOH658 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 504 |
| Chain | Residue |
| A | ASN315 |
| A | ALA318 |
| A | GLY321 |
| A | GLY356 |
| A | ASP357 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE UD1 B 501 |
| Chain | Residue |
| B | ASN24 |
| B | TRP96 |
| B | ARG121 |
| B | PRO122 |
| B | VAL123 |
| B | ASP124 |
| B | LEU125 |
| B | HIS126 |
| B | LYS161 |
| B | SER163 |
| B | VAL164 |
| B | GLY165 |
| B | THR305 |
| B | ASP306 |
| B | ILE328 |
| B | PHE329 |
| B | HOH604 |
| B | HOH624 |
| B | HOH628 |
| B | HOH636 |
| B | HOH646 |
| B | HOH649 |
| B | HOH661 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FFQ B 502 |
| Chain | Residue |
| B | THR90 |
| B | MET91 |
| B | ARG92 |
| B | CYS116 |
| B | ARG398 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 503 |
| Chain | Residue |
| B | ASN315 |
| B | ALA318 |
| B | GLY321 |
| B | GLY356 |
| B | ASP357 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE UD1 C 501 |
| Chain | Residue |
| C | ASN24 |
| C | TRP96 |
| C | ARG121 |
| C | PRO122 |
| C | VAL123 |
| C | ASP124 |
| C | LEU125 |
| C | HIS126 |
| C | LYS161 |
| C | SER163 |
| C | VAL164 |
| C | GLY165 |
| C | THR305 |
| C | ASP306 |
| C | ILE328 |
| C | HOH629 |
| C | HOH641 |
| C | HOH643 |
| C | HOH645 |
| C | HOH651 |
| C | HOH652 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FFQ C 502 |
| Chain | Residue |
| C | THR90 |
| C | MET91 |
| C | ARG92 |
| C | CYS116 |
| C | ARG398 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 503 |
| Chain | Residue |
| C | ASP357 |
| C | ASN315 |
| C | ALA318 |
| C | GLY321 |
| C | GLY356 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 504 |
| Chain | Residue |
| C | GLU330 |
| C | HOH658 |
| D | GLU330 |
| D | HOH668 |
| D | HOH669 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE UD1 D 501 |
| Chain | Residue |
| D | ASN24 |
| D | TRP96 |
| D | ARG121 |
| D | PRO122 |
| D | VAL123 |
| D | ASP124 |
| D | LEU125 |
| D | LYS161 |
| D | SER163 |
| D | VAL164 |
| D | GLY165 |
| D | THR305 |
| D | ASP306 |
| D | ILE328 |
| D | PHE329 |
| D | HOH613 |
| D | HOH618 |
| D | HOH641 |
| D | HOH663 |
| D | HOH664 |
| D | HOH678 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FFQ D 502 |
| Chain | Residue |
| D | THR90 |
| D | MET91 |
| D | ARG92 |
| D | CYS116 |
| D | ARG398 |
| D | HOH619 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 503 |
| Chain | Residue |
| D | ASN315 |
| D | ALA318 |
| D | GLY321 |
| D | GLY356 |
| D | ASP357 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00111 |
| Chain | Residue | Details |
| A | CYS116 | |
| B | CYS116 | |
| C | CYS116 | |
| D | CYS116 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0007744|PDB:4R7U |
| Chain | Residue | Details |
| A | LYS23 | |
| B | ILE328 | |
| C | LYS23 | |
| C | ARG121 | |
| C | LYS161 | |
| C | ASP306 | |
| C | ILE328 | |
| D | LYS23 | |
| D | ARG121 | |
| D | LYS161 | |
| D | ASP306 | |
| A | ARG121 | |
| D | ILE328 | |
| A | LYS161 | |
| A | ASP306 | |
| A | ILE328 | |
| B | LYS23 | |
| B | ARG121 | |
| B | LYS161 | |
| B | ASP306 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111 |
| Chain | Residue | Details |
| A | ARG92 | |
| B | ARG92 | |
| C | ARG92 | |
| D | ARG92 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111 |
| Chain | Residue | Details |
| A | CYS116 | |
| B | CYS116 | |
| C | CYS116 | |
| D | CYS116 |
