3SU9
E. Cloacae MURA in complex with UDP-N-acetylmuramic acid and covalent adduct of PEP with Cys115
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 | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 420 |
Chain | Residue |
A | ARG91 |
A | ILE94 |
A | ARG120 |
A | HIS125 |
A | GLY164 |
A | EPZ427 |
A | HOH450 |
A | HOH522 |
A | HOH589 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 421 |
Chain | Residue |
A | ARG252 |
A | TRP279 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 422 |
Chain | Residue |
A | LEU138 |
A | HIS344 |
A | HOH437 |
A | HOH614 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 423 |
Chain | Residue |
A | ARG288 |
A | LYS290 |
A | GLU318 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 424 |
Chain | Residue |
A | ALA102 |
A | ARG103 |
A | GLY149 |
A | ARG150 |
A | HOH596 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 425 |
Chain | Residue |
A | SER81 |
A | GLU140 |
A | TYR142 |
A | LYS144 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT A 426 |
Chain | Residue |
A | GLN108 |
A | LYS144 |
site_id | AC8 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE EPZ A 427 |
Chain | Residue |
A | LYS22 |
A | ASN23 |
A | TRP95 |
A | ALA119 |
A | ARG120 |
A | PRO121 |
A | VAL122 |
A | ASP123 |
A | LEU124 |
A | LYS160 |
A | SER162 |
A | VAL163 |
A | GLY164 |
A | ASP305 |
A | ILE327 |
A | PHE328 |
A | ARG331 |
A | LEU370 |
A | EDO420 |
A | HOH430 |
A | HOH453 |
A | HOH503 |
A | HOH515 |
A | HOH522 |
A | HOH534 |
A | HOH537 |
A | HOH539 |
A | HOH541 |
A | HOH590 |
A | HOH644 |
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 | QPA115 |
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 | QPA115 |
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 | QPA115 | 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 |