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3H1M

Crystal structure of mannose 6-phosphate isomerase (holo; zinc bound)

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 Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 392
ChainResidue
ALEU94
ASER95
AGLN97
AHIS255
AALA256
ATYR257
AZN395
AHOH400
AHOH491

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 393
ChainResidue
AASN6
ALYS307
ASER308
AGLY309
AEDO394

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 394
ChainResidue
AASN6
AGLY364
AEDO393
AHOH447

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 395
ChainResidue
AHIS99
AGLU134
AHIS255
AEDO392
AHOH400

Functional Information from PROSITE/UniProt
site_idPS00965
Number of Residues9
DetailsPMI_I_1 Phosphomannose isomerase type I signature 1. YkDpNHKPE
ChainResidueDetails
ATYR126-GLU134

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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pmi
ChainResidueDetails
AGLN97
AGLU264
AARG274

246704

PDB entries from 2025-12-24

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