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2WFP

Crystal structure of mannose 6-phosphate isomerase (apo form) 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 EDO A 1392
ChainResidue
AARG353
ALYS354
AASP355
APRO375
AASN377
AHOH2359

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1393
ChainResidue
ATHR278
AEDO1403
AHOH2262
AHOH2360
ALYS195
AASP227
ASER228

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1394
ChainResidue
ASER95
AGLN97
AHOH2106

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1395
ChainResidue
AILE96
APHE184
ASER228
AGLY229
APHE231
ASER232
AALA275

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1396
ChainResidue
AASN6
ALYS307
ASER308
AGLY309
AEDO1400
AHOH2364

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1397
ChainResidue
AALA185
AASN189
AILE284

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1398
ChainResidue
AARG77
AVAL155
ALEU172
APRO175
AEDO1405
AHOH2361
AHOH2362

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 1399
ChainResidue
AHOH2363

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1400
ChainResidue
AASN6
AGLY364
AEDO1396
AHOH2014
AHOH2364

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1401
ChainResidue
AALA310
AGLU311
AHIS326
ASER334
AHOH2315
AHOH2365

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1402
ChainResidue
AASN104
ALYS111
ATYR126
AGLU286
AASN290
AHOH2366

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1403
ChainResidue
AMET190
AGLN191
ALYS195
AEDO1393
AHOH2226
AHOH2229
AHOH2368

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1404
ChainResidue
AGLN97
AHIS99
AGLU134
ALEU249
AHIS255
AGLU264

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1405
ChainResidue
AASN76
AEDO1398
AHOH2093
AHOH2368
AHOH2369
AHOH2370

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1406
ChainResidue
AALA298
AGLY299
AGLU300
ALEU301
ALEU302

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1407
ChainResidue
AALA40
APRO42
AARG59
AGLU80
ALEU81
AASN268
AHOH2372

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
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AARG274

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

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

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PDB entries from 2024-07-10

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