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3GP3

Crystal structure of phosphoglyceromutase from Burkholderia pseudomallei with 2-phosphoserine

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
C0003824molecular_functioncatalytic activity
C0004619molecular_functionphosphoglycerate mutase activity
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016853molecular_functionisomerase activity
C0016868molecular_functionintramolecular phosphotransferase activity
D0003824molecular_functioncatalytic activity
D0004619molecular_functionphosphoglycerate mutase activity
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0016853molecular_functionisomerase activity
D0016868molecular_functionintramolecular phosphotransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PG4 A 250
ChainResidue
AASP51
AALA173
ALYS175

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO3 A 251
ChainResidue
AGLY183
ASEP252
AHOH274
AARG8
AHIS9
AASN15
AARG60
AGLU87
AHIS182

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SEP A 252
ChainResidue
AARG8
AASN15
AARG19
ATHR21
AGLY22
AGLU87
AARG88
ATYR90
ALYS98
AARG114
AARG115
AASN184
APO3251
AHOH278

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PG4 B 250
ChainResidue
BASP51
BALA173
BLYS175

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO3 B 251
ChainResidue
BARG8
BHIS9
BASN15
BARG60
BGLU87
BHIS182
BGLY183
BSEP252
BHOH279

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SEP B 252
ChainResidue
BARG8
BASN15
BARG19
BTHR21
BGLY22
BGLU87
BTYR90
BLYS98
BARG114
BARG115
BASN184
BPO3251
BHOH299

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 C 250
ChainResidue
CASP51
CALA173
CLYS175
CHOH552

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 C 251
ChainResidue
CILE196
CLEU204
CHIS225
CHOH332
CHOH556

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO3 C 252
ChainResidue
CARG8
CHIS9
CASN15
CARG60
CGLU87
CHIS182
CGLY183
CSEP253

site_idBC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SEP C 253
ChainResidue
CARG8
CASN15
CARG19
CPHE20
CTHR21
CGLY22
CGLU87
CTYR90
CLYS98
CARG114
CARG115
CASN184
CPO3252
CHOH305

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 D 250
ChainResidue
DASP51
DALA173
DLYS175
DHOH601

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PG4 D 251
ChainResidue
DILE190
DILE196
DTYR214
DHIS225
DTYR227
DHOH282
DHOH374
DHOH706

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO3 D 252
ChainResidue
DHIS182
DGLY183
DSEP253
DHOH290
DARG8
DHIS9
DASN15
DARG60
DGLU87

site_idBC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SEP D 253
ChainResidue
DARG8
DASN15
DARG19
DPHE20
DTHR21
DGLY22
DGLU87
DTYR90
DLYS98
DARG114
DARG115
DASN184
DPO3252
DHOH295

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 Residues4
DetailsActive site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues48
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21904048","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FDZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues60
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
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

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
CHIS182
CARG60
CGLU87
CHIS9

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
DHIS182
DARG60
DGLU87
DHIS9

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PDB entries from 2025-12-03

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