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3GP5

Crystal structure of phosphoglyceromutase from Burkholderia pseudomallei with 3-phosphoglyceric acid and vanadate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004619molecular_functionphosphoglycerate mutase activity
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
B0003824molecular_functioncatalytic activity
B0004619molecular_functionphosphoglycerate mutase activity
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PG6 A 250
ChainResidue
AILE190
AASP194
AILE196
ALEU204
ATYR214
AHIS225
ATYR227
AHOH336
AHOH337

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE VO4 A 251
ChainResidue
AARG8
AHIS9
AASN15
AARG60
AGLU87
AHIS182
AGLY183
A3PG252
AHOH264

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 3PG A 252
ChainResidue
ATHR21
AGLY22
AGLU87
ATYR90
ALYS98
AARG114
AARG115
AASN184
AVO4251
AHOH254
AHOH265
AHOH292
AHOH324

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 B 250
ChainResidue
ALYS140
BASP51
BALA173
BLYS175

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PG4 B 251
ChainResidue
BILE190
BASP194
BILE196
BTYR214
BHIS225
BTYR227
BHOH332

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE VO4 B 252
ChainResidue
BARG8
BHIS9
BASN15
BARG60
BGLU87
BHIS182
BGLY183
B3PG253
BHOH294

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 3PG B 253
ChainResidue
BTHR21
BGLY22
BGLU87
BTYR90
BLYS98
BARG114
BARG115
BASN184
BVO4252
BHOH280
BHOH295

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEsTwN
ChainResidueDetails
ALEU6-ASN15

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21904048","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FDZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AHIS182
AARG60
AGLU87
AHIS9

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
BHIS182
BARG60
BGLU87
BHIS9

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PDB entries from 2025-12-10

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