1EYN
Structure of mura liganded with the extrinsic fluorescence probe ANS
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 | 13 |
| Details | BINDING SITE FOR RESIDUE 2AN A 550 |
| Chain | Residue |
| A | TRP71 |
| A | PRO112 |
| A | GLY113 |
| A | ARG120 |
| A | HOH661 |
| A | ILE72 |
| A | ASP73 |
| A | VAL87 |
| A | LYS88 |
| A | MET90 |
| A | ARG91 |
| A | SER93 |
| A | LEU111 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 551 |
| Chain | Residue |
| A | ARG91 |
| A | ILE94 |
| A | TRP95 |
| A | HOH792 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 552 |
| Chain | Residue |
| A | ASP159 |
| A | ALA291 |
| A | HOH587 |
| A | HOH767 |
| A | HOH877 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20392080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LTH","evidenceCode":"ECO:0007744"}]} |
| 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":"3SWQ","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 | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20392080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LTH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SWQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SWQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"2-(S-cysteinyl)pyruvic acid O-phosphothioketal","evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"}]} |
| 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 | ASP305 | |
| A | ARG397 | |
| A | CYS115 | |
| A | ASN23 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 369 |
| Chain | Residue | Details |
| A | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| A | ASN23 | electrostatic stabiliser, hydrogen bond donor |
| A | ALA119 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| A | LEU124 | electrostatic stabiliser, proton acceptor, proton donor |
| A | GLN309 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG401 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
