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3FDZ

Crystal structure of phosphoglyceromutase from burkholderia pseudomallei 1710b with bound 2,3-diphosphoglyceric acid and 3-phosphoglyceric acid

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 Residues17
DetailsBINDING SITE FOR RESIDUE DG2 A1001
ChainResidue
AARG8
AARG114
AARG115
AHIS182
AGLY183
AASN184
AHOH349
AHOH350
AHOH355
AHIS9
AASN15
ATHR21
AGLY22
AARG60
AGLU87
ATYR90
ALYS98

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG A1002
ChainResidue
AASP194
ALEU204
ATYR214
AHIS225
ATYR227
AHOH259

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 3PG B1001
ChainResidue
BNEP9
BARG19
BPHE20
BTHR21
BGLY22
BGLU87
BTYR90
BLYS98
BARG114
BARG115
BASN184
BHOH330

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG B1002
ChainResidue
BILE190
BLEU204
BTYR214
BHIS225
BTYR227
BHOH366

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEsTwN
ChainResidueDetails
BLEU6-ASN15
ALEU6-ASN15

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000269|PubMed:21904048
ChainResidueDetails
BNEP9

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
BGLU87

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:21904048, ECO:0007744|PDB:3FDZ
ChainResidueDetails
BASN15
BARG8
BTYR90
BLYS98
BARG114
BARG115
BHIS182
BGLY183
BASN184
BNEP9
BTHR21
BGLY22
BARG60
BGLU87

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
BHIS182

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PDB entries from 2024-06-12

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