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5ZVU

Crystal structure of K132A mutant of phosphomannose isomerase from Salmonella typhimurium

Functional Information from GO Data
ChainGOidnamespacecontents
A0004476molecular_functionmannose-6-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008270molecular_functionzinc ion binding
A0009298biological_processGDP-mannose biosynthetic process
A0016853molecular_functionisomerase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS99
AGLU134
AHIS255
AEDO402

site_idAC2
Number of Residues7
Detailsbinding site for residue EDO A 402
ChainResidue
ATYR257
AZN401
ALEU94
ASER95
AGLN97
AHIS255
AALA256

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 403
ChainResidue
AASN10
AGLN31
AHOH562
AHOH583
AHOH624

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 404
ChainResidue
AARG149
AASN237
AVAL238
AHOH520

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 405
ChainResidue
ATYR11
ATRP13

Functional Information from PROSITE/UniProt
site_idPS00966
Number of Residues26
DetailsPMI_I_2 Phosphomannose isomerase type I signature 2. HAYLqGvaLEvMAnSDNvLRAGlTPK
ChainResidueDetails
AHIS255-LYS280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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