4E7G
E. cloacae C115D/R120A MurA in the unliganded state
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 | 8 |
| Details | BINDING SITE FOR RESIDUE PEG A 501 |
| Chain | Residue |
| A | ARG227 |
| A | PRO230 |
| A | ASN253 |
| A | ALA254 |
| A | ASP278 |
| A | HOH680 |
| A | HOH899 |
| A | HOH1102 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 502 |
| Chain | Residue |
| A | ARG227 |
| A | HOH643 |
| A | GLN42 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | GLN106 |
| A | GLY107 |
| A | GLN108 |
| A | HOH673 |
| A | HOH1047 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | ALA200 |
| A | LEU201 |
| A | GLY222 |
| A | GLY223 |
| A | HOH656 |
| A | HOH1008 |
| A | HOH1097 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | ARG91 |
| A | ALA92 |
| A | TRP95 |
| A | HOH627 |
| A | HOH817 |
| A | HOH1011 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 506 |
| Chain | Residue |
| A | GLU37 |
| A | THR89 |
| A | ARG91 |
| A | ARG397 |
| A | HOH627 |
| A | HOH694 |
| A | HOH721 |
| A | HOH751 |
| A | HOH1067 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 507 |
| Chain | Residue |
| A | THR304 |
| A | ASP305 |
| A | ALA331 |
| A | HOH893 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 508 |
| Chain | Residue |
| A | ALA291 |
| A | VAL292 |
| A | THR293 |
| A | THR320 |
| A | HOH787 |
| A | HOH992 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 509 |
| Chain | Residue |
| A | ASN23 |
| A | TRP95 |
| A | VAL163 |
| A | HOH639 |
| A | HOH791 |
| A | HOH817 |
| A | HOH1092 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 510 |
| Chain | Residue |
| A | ALA261 |
| A | LYS265 |
| A | ALA301 |
| A | PHE302 |
| A | HOH654 |
| A | HOH757 |
| A | HOH789 |
| A | HOH853 |
| A | HOH857 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 511 |
| Chain | Residue |
| A | ASN23 |
| A | GLU190 |
| A | ARG232 |
| A | ASP305 |
| A | HOH652 |
| A | HOH864 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 512 |
| Chain | Residue |
| A | LYS46 |
| A | LEU47 |
| A | LYS48 |
| A | ASP51 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 513 |
| Chain | Residue |
| A | ARG187 |
| A | THR210 |
| A | ASP211 |
| A | HOH1103 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 514 |
| Chain | Residue |
| A | ALA120 |
| A | ASP123 |
| A | LEU138 |
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 | ASP115 |
| 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 | ALA120 | |
| 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 | ASP115 |
Catalytic Information from CSA
| 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 | ASP115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| A | ALA120 | 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 |
