2YVW
Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Aquifex aeolicus VF5
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 511 |
| Chain | Residue |
| A | ARG98 |
| A | MET99 |
| A | ARG100 |
| A | ARG403 |
| A | HOH649 |
| A | HOH705 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE EPU A 501 |
| Chain | Residue |
| A | ARG129 |
| A | PRO130 |
| A | ILE131 |
| A | ASP132 |
| A | GLN133 |
| A | LEU168 |
| A | VAL169 |
| A | THR170 |
| A | VAL171 |
| A | THR172 |
| A | ASP311 |
| A | ILE333 |
| A | PHE334 |
| A | VAL353 |
| A | LEU376 |
| A | HOH605 |
| A | HOH610 |
| A | HOH616 |
| A | HOH625 |
| A | HOH629 |
| A | HOH634 |
| A | HOH636 |
| A | HOH639 |
| A | HOH641 |
| A | HOH642 |
| A | HOH649 |
| A | HOH806 |
| A | HOH807 |
| A | HOH809 |
| A | LYS31 |
| A | ASN32 |
| A | ALA101 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00111","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2YVW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SWG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00111","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YVW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SWG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"2-(S-cysteinyl)pyruvic acid O-phosphothioketal","evidences":[{"source":"HAMAP-Rule","id":"MF_00111","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uae |
| Chain | Residue | Details |
| A | ASP311 | |
| A | ARG403 | |
| A | ASN32 | |
| A | CYS124 |
