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5ZVR

Crystal structure of R274A 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 Residues6
Detailsbinding site for residue ZN A 401
ChainResidue
AGLN97
AHIS99
AGLU134
AHIS255
AEDO407
AHOH503

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 402
ChainResidue
APRO305
AHOH649
AHOH652
AASN10
APRO32
ALEU302

site_idAC3
Number of Residues2
Detailsbinding site for residue EDO A 403
ChainResidue
ATRP13
AHOH521

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO A 404
ChainResidue
APHE184
ALEU187
ASER228
AGLY229
APHE231
ASER232
AHOH625

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 405
ChainResidue
APHE137
AALA138
AGLY244
AARG383

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO A 406
ChainResidue
AGLY163
ASER166
AARG197
AHOH693
AHOH695
AHOH728

site_idAC7
Number of Residues7
Detailsbinding site for residue EDO A 407
ChainResidue
ALEU94
ASER95
AGLN97
AALA256
ATYR257
AZN401
AHOH503

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AALA274

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLN97
AHIS99
AGLU134
AHIS255

222415

PDB entries from 2024-07-10

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