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2HHJ

Human bisphosphoglycerate mutase complexed with 2,3-bisphosphoglycerate (15 days)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004082molecular_functionbisphosphoglycerate mutase activity
A0004619molecular_functionphosphoglycerate mutase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006096biological_processglycolytic process
A0007585biological_processrespiratory gaseous exchange by respiratory system
A0016787molecular_functionhydrolase activity
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0070062cellular_componentextracellular exosome
A1901136biological_processcarbohydrate derivative catabolic process
B0003824molecular_functioncatalytic activity
B0004082molecular_functionbisphosphoglycerate mutase activity
B0004619molecular_functionphosphoglycerate mutase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006096biological_processglycolytic process
B0007585biological_processrespiratory gaseous exchange by respiratory system
B0016787molecular_functionhydrolase activity
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0070062cellular_componentextracellular exosome
B1901136biological_processcarbohydrate derivative catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HAI A 2000
ChainResidue
ALEU95
AHIS107
APRO124

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE DG2 B 2200
ChainResidue
BARG62
BGLU89
BTYR92
BARG100
BARG116
BARG117
BHIS188
BGLY189
BASN190
BHOH3212
BHOH3345
BHOH3422
BHOH3423
BARG10
BNEP11
BASN17
BPHE22
BCYS23
BSER24

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE DG2 A 2201
ChainResidue
AARG10
ANEP11
AASN17
APHE22
ACYS23
ASER24
AARG62
AGLU89
ATYR92
AARG100
AARG116
AARG117
AHIS188
AGLY189
AASN190
AHOH3236
AHOH3238
AHOH3465
AHOH3466

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 3PG A 3200
ChainResidue
AARG10
ANEP11
APHE22
ACYS23
ASER24
AGLU89
ATYR92
AARG100
AARG116
AARG117
AASN190
AHOH3236
AHOH3238
AHOH3465
AHOH3466

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 3PG B 3201
ChainResidue
BARG10
BNEP11
BPHE22
BCYS23
BSER24
BGLU89
BTYR92
BARG100
BARG116
BARG117
BASN190
BHOH3212
BHOH3345
BHOH3422
BHOH3423

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. MlRHGEgAwN
ChainResidueDetails
AMET8-ASN17

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"17052986","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17052986","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17052986","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsSite: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"9832630","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"17052986","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"9832630","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"9832630","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AARG62
AHIS188
AGLU89

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
BARG62
BHIS188
BGLU89

247536

PDB entries from 2026-01-14

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