1EJC
Crystal structure of unliganded mura (type2)
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 | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 701 |
Chain | Residue |
A | MET1 |
A | ASP2 |
A | TYR393 |
A | HOH502 |
A | HOH731 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 601 |
Chain | Residue |
A | HOH694 |
A | HOH706 |
A | HOH809 |
A | ARG252 |
A | TRP279 |
A | ARG340 |
A | GLY362 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 602 |
Chain | Residue |
A | HIS344 |
A | HIS355 |
A | GLY356 |
A | HOH733 |
A | HOH819 |
A | HOH935 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 603 |
Chain | Residue |
A | ARG91 |
A | ALA92 |
A | ILE94 |
A | TRP95 |
A | HIS125 |
A | GLY164 |
A | HOH508 |
A | HOH764 |
A | HOH847 |
A | HOH905 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 604 |
Chain | Residue |
A | PHE104 |
A | ASN330 |
A | PHE332 |
A | MET333 |
A | PRO336 |
A | HOH455 |
A | HOH838 |
A | HOH920 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH |
Chain | Residue | Details |
A | CYS115 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ |
Chain | Residue | Details |
A | LYS22 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111 |
Chain | Residue | Details |
A | ARG91 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH, ECO:0007744|PDB:3SWQ |
Chain | Residue | Details |
A | ARG120 | |
A | ASP305 | |
A | ILE327 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ |
Chain | Residue | Details |
A | LYS160 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269|PubMed:22378791 |
Chain | Residue | Details |
A | CYS115 |
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 | CYS115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
A | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
A | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |