1DLG
CRYSTAL STRUCTURE OF THE C115S ENTEROBACTER CLOACAE MURA IN THE UN-LIGANDED 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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1500 |
| Chain | Residue |
| A | GLU135 |
| A | LYS137 |
| A | LYS144 |
| A | HAI1424 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1501 |
| Chain | Residue |
| B | HAI1420 |
| A | ARG252 |
| A | ASP278 |
| A | HOH658 |
| B | ARG252 |
| B | ASN253 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1502 |
| Chain | Residue |
| A | ARG401 |
| A | GLU403 |
| A | ASP404 |
| A | ARG407 |
| A | ARG415 |
| A | HOH695 |
| A | HOH917 |
| A | HOH984 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1503 |
| Chain | Residue |
| A | SER162 |
| A | VAL163 |
| A | GLY164 |
| A | HOH460 |
| A | HOH749 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1504 |
| Chain | Residue |
| B | ASN23 |
| B | ASP305 |
| B | ARG371 |
| B | HOH454 |
| B | HOH728 |
| B | HOH980 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1506 |
| Chain | Residue |
| A | GLY118 |
| A | ALA119 |
| B | ALA119 |
| B | ASP159 |
| B | LYS160 |
| B | HOH1082 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1507 |
| Chain | Residue |
| B | ALA92 |
| B | TRP95 |
| B | HOH520 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1508 |
| Chain | Residue |
| B | GLY319 |
| B | THR320 |
| B | HIS355 |
| B | HOH589 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1509 |
| Chain | Residue |
| A | HOH887 |
| B | TYR393 |
| B | HIS394 |
| B | ARG397 |
| B | HOH477 |
| B | HOH891 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HAI B 1420 |
| Chain | Residue |
| A | VAL250 |
| A | TRP279 |
| B | TRP279 |
| B | HOH552 |
| B | PO41501 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HAI B 1422 |
| Chain | Residue |
| A | VAL250 |
| A | GLU274 |
| A | SER281 |
| B | VAL250 |
| B | GLU274 |
| B | SER281 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HAI A 1424 |
| Chain | Residue |
| A | PHE80 |
| A | GLU135 |
| A | LYS144 |
| A | ASN148 |
| A | PO41500 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH |
| Chain | Residue | Details |
| A | SER115 | |
| B | SER115 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ |
| Chain | Residue | Details |
| A | LYS22 | |
| B | LYS22 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111 |
| Chain | Residue | Details |
| A | ARG91 | |
| B | ARG91 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| 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 | |
| B | ARG120 | |
| B | ASP305 | |
| B | ILE327 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ |
| Chain | Residue | Details |
| A | LYS160 | |
| B | LYS160 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269|PubMed:22378791 |
| Chain | Residue | Details |
| A | SER115 | |
| B | SER115 |
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 | SER115 | |
| A | ASN23 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uae |
| Chain | Residue | Details |
| B | ASP305 | |
| B | ARG397 | |
| B | SER115 | |
| B | 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 | SER115 | 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 |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 369 |
| Chain | Residue | Details |
| B | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| B | ASN23 | electrostatic stabiliser, hydrogen bond donor |
| B | SER115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| B | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
| B | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
