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1TZF

X-ray Crystal Structure of alpha-D-glucose-1-phosphate cytidylyltransferase from Salmonella typhi

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0009058biological_processbiosynthetic process
A0009103biological_processlipopolysaccharide biosynthetic process
A0009243biological_processO antigen biosynthetic process
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0046872molecular_functionmetal ion binding
A0047343molecular_functionglucose-1-phosphate cytidylyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AASP131
AASP236
AC5G401
AHOH663
AHOH664

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE C5G A 401
ChainResidue
ALYS25
APRO26
ASER106
AARG111
ATYR129
AGLY130
AASP131
APHE163
AGLY164
AGLU178
ALYS179
AASN188
AGLU210
ATRP232
AASP236
AMG403
AHOH523
AHOH613
AHOH663
AHOH664
ALEU8
AALA9
AGLY10
AGLY11

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15292268","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15634670","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15634670","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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