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5UJS

2.45 Angstrom Resolution Crystal Structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Campylobacter jejuni.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0008360biological_processregulation of cell shape
A0008760molecular_functionUDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0019277biological_processUDP-N-acetylgalactosamine biosynthetic process
A0051301biological_processcell division
A0071555biological_processcell wall organization
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0008360biological_processregulation of cell shape
B0008760molecular_functionUDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016740molecular_functiontransferase activity
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0019277biological_processUDP-N-acetylgalactosamine biosynthetic process
B0051301biological_processcell division
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 501
ChainResidue
AGLY206
AILE207

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00111
ChainResidueDetails
ACYS116
BCYS116

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111
ChainResidueDetails
ALYS22
BLEU327
AARG92
AARG121
AASP305
ALEU327
BLYS22
BARG92
BARG121
BASP305

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111
ChainResidueDetails
ACYS116
BCYS116

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PDB entries from 2024-07-24

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