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 |