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1QHF

YEAST PHOSPHOGLYCERATE MUTASE-3PG COMPLEX STRUCTURE TO 1.7 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004619molecular_functionphosphoglycerate mutase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005758cellular_componentmitochondrial intermembrane space
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
B0003824molecular_functioncatalytic activity
B0004619molecular_functionphosphoglycerate mutase activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005741cellular_componentmitochondrial outer membrane
B0005758cellular_componentmitochondrial intermembrane space
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 248
ChainResidue
A3PG252
AHOH331
AHIS8
ASER11
AASN14
ATHR20
AARG59

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 249
ChainResidue
BHIS8
BSER11
BASN14
BTHR20
B3PG253
BHOH348
BHOH349
BHOH352

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 250
ChainResidue
BTYR89
BARG113
BHOH347
BHOH369

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 251
ChainResidue
APHE19
ATYR89
ALYS97
AARG113
AVAL240
AHOH286

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 3PG A 252
ChainResidue
AARG7
AHIS8
AGLY9
AGLN10
ASER11
AASN14
ATHR20
AARG59
ATHR207
ASO4248
AHOH331
AHOH345

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 3PG B 253
ChainResidue
BARG7
BHIS8
BGLY9
BGLN10
BSER11
BASN14
BTHR20
BARG59
BTHR207
BSO4249
BHOH348
BHOH349
BHOH352

site_idPGA
Number of Residues2
Details3PG BINDING SITE
ChainResidue
AHIS8
AHIS181

site_idPGB
Number of Residues2
Details3PG BINDING SITE
ChainResidue
BHIS8
BHIS181

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LvRHGQsEwN
ChainResidueDetails
ALEU5-ASN14

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:10064712, ECO:0000269|PubMed:10531478, ECO:0000269|PubMed:6115412, ECO:0000269|PubMed:9512715
ChainResidueDetails
AGLY9
BGLY9

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:10064712
ChainResidueDetails
AARG87
BARG87

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:10531478, ECO:0000269|PubMed:6115412
ChainResidueDetails
AHIS8
BHIS8

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:10531478
ChainResidueDetails
AGLY21
BGLY21

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10531478
ChainResidueDetails
AALA60
BALA60

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:6115412
ChainResidueDetails
AARG87
AASN183
BARG87
BASN183

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10369755
ChainResidueDetails
AALA98
AARG114
BALA98
BARG114

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:10064712
ChainResidueDetails
AGLY182
BGLY182

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358
ChainResidueDetails
AGLU12
ALEU185
BGLU12
BLEU185

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19779198
ChainResidueDetails
APRO49
BPRO49

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
APHE116
BPHE116

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER127
BSER127

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
APRO128
BPRO128

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
AASP197
BASP197

site_idSWS_FT_FI15
Number of Residues14
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
AGLY31
BLEU57
BALA71
BTYR139
BTHR175
BHIS191
ALEU57
AALA71
ATYR139
ATHR175
AHIS191
BGLY31

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 504
ChainResidueDetails
AGLY9covalent catalysis
AALA60electrostatic stabiliser
AARG87proton donor, proton shuttle (general acid/base)
AGLY182electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 504
ChainResidueDetails
BGLY9covalent catalysis
BALA60electrostatic stabiliser
BARG87proton donor, proton shuttle (general acid/base)
BGLY182electrostatic stabiliser

218853

PDB entries from 2024-04-24

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