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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4PGM

SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE

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
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0061621biological_processcanonical glycolysis
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
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0061621biological_processcanonical glycolysis
C0003824molecular_functioncatalytic activity
C0004619molecular_functionphosphoglycerate mutase activity
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005741cellular_componentmitochondrial outer membrane
C0005758cellular_componentmitochondrial intermembrane space
C0005829cellular_componentcytosol
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016853molecular_functionisomerase activity
C0016868molecular_functionintramolecular phosphotransferase activity
C0061621biological_processcanonical glycolysis
D0003824molecular_functioncatalytic activity
D0004619molecular_functionphosphoglycerate mutase activity
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005741cellular_componentmitochondrial outer membrane
D0005758cellular_componentmitochondrial intermembrane space
D0005829cellular_componentcytosol
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0016853molecular_functionisomerase activity
D0016868molecular_functionintramolecular phosphotransferase activity
D0061621biological_processcanonical glycolysis
Functional Information from PDB Data
site_idCIC
Number of Residues4
DetailsCATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME.
ChainResidue
AHIS8
AHIS181
AARG7
AARG59
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 Residues4
DetailsActive site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"10064712","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10531478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6115412","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9512715","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"10064712","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10369755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10531478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6115412","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10369755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10531478","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10531478","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10369755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6115412","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10369755","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"10064712","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues28
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AHIS181
AHIS8
AGLU86
AARG59
site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
BHIS181
BHIS8
BGLU86
BARG59
site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
CHIS181
CHIS8
CGLU86
CARG59
site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
DHIS181
DHIS8
DGLU86
DARG59
site_idMCSA1
Number of Residues4
DetailsM-CSA 504
ChainResidueDetails
AHIS8covalent catalysis
AARG59electrostatic stabiliser
AGLU86proton donor, proton shuttle (general acid/base)
AHIS181electrostatic stabiliser
site_idMCSA2
Number of Residues4
DetailsM-CSA 504
ChainResidueDetails
BHIS8covalent catalysis
BARG59electrostatic stabiliser
BGLU86proton donor, proton shuttle (general acid/base)
BHIS181electrostatic stabiliser
site_idMCSA3
Number of Residues4
DetailsM-CSA 504
ChainResidueDetails
CHIS8covalent catalysis
CARG59electrostatic stabiliser
CGLU86proton donor, proton shuttle (general acid/base)
CHIS181electrostatic stabiliser
site_idMCSA4
Number of Residues4
DetailsM-CSA 504
ChainResidueDetails
DHIS8covalent catalysis
DARG59electrostatic stabiliser
DGLU86proton donor, proton shuttle (general acid/base)
DHIS181electrostatic stabiliser

245011

PDB entries from 2025-11-19

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