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3GW8

Crystal structure of phosphoglyceromutase from Burkholderia pseudomallei with vanadate and glycerol

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
A0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
B0003824molecular_functioncatalytic activity
B0004619molecular_functionphosphoglycerate mutase activity
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE VO4 A 401
ChainResidue
AARG8
AHIS9
AASN15
AARG60
AGLU87
AHIS182
AGLY183
AHOH313
AGOL402

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AARG8
AASN15
AARG19
APHE20
ATHR21
AGLY22
AGLU87
ATYR90
AHOH255
AHOH383
AVO4401
AVO4403

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE VO4 A 403
ChainResidue
APHE20
ATYR90
ALYS98
AASN184
AHOH255
AGOL402

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 A 501
ChainResidue
AILE196
ALEU204
AHIS225
AHOH414

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PG4 A 502
ChainResidue
AALA173
ALYS175

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 A 250
ChainResidue
ALYS140
AHOH317
BASP51
BLYS175

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE VO4 B 401
ChainResidue
BARG8
BHIS9
BASN15
BARG60
BGLU87
BHIS182
BGLY183
BHOH277
BGOL402

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL B 402
ChainResidue
BARG8
BASN15
BARG19
BPHE20
BTHR21
BGLY22
BGLU87
BTYR90
BHOH342
BVO4401
BVO4403

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE VO4 B 403
ChainResidue
BTYR90
BLYS98
BARG114
BARG115
BASN184
BGOL402

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PG4 B 501
ChainResidue
BASP194
BILE196
BLEU204
BTYR214
BHIS225
BTYR227
BHOH282

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
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000269|PubMed:21904048
ChainResidueDetails
AHIS9
BHIS9

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
AGLU87
BGLU87

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:21904048, ECO:0007744|PDB:3FDZ
ChainResidueDetails
AARG8
BARG60
BGLU87
BLYS98
BARG114
BGLY183
AHIS9
AASN15
AGLY22
ATYR90
AARG115
ATHR21
AHIS182
AASN184
BHIS9
BASN15
BGLY22
BTYR90
BARG115
BHIS182
BASN184
AARG60
AGLU87
ALYS98
AARG114
AGLY183
BARG8
BTHR21

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
AHIS182
BHIS182

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 2024-07-24

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