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1R2S

CRYSTAL STRUCTURE OF RABBIT MUSCLE TRIOSEPHOSPHATE ISOMERASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0008929molecular_functionmethylglyoxal synthase activity
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
A0019242biological_processmethylglyoxal biosynthetic process
A0019563biological_processglycerol catabolic process
A0019682biological_processglyceraldehyde-3-phosphate metabolic process
A0031625molecular_functionubiquitin protein ligase binding
A0042803molecular_functionprotein homodimerization activity
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
A0061621biological_processcanonical glycolysis
B0004807molecular_functiontriose-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006006biological_processglucose metabolic process
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0008929molecular_functionmethylglyoxal synthase activity
B0016829molecular_functionlyase activity
B0016853molecular_functionisomerase activity
B0019242biological_processmethylglyoxal biosynthetic process
B0019563biological_processglycerol catabolic process
B0019682biological_processglyceraldehyde-3-phosphate metabolic process
B0031625molecular_functionubiquitin protein ligase binding
B0042803molecular_functionprotein homodimerization activity
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0061621biological_processcanonical glycolysis
C0004807molecular_functiontriose-phosphate isomerase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006006biological_processglucose metabolic process
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0008929molecular_functionmethylglyoxal synthase activity
C0016829molecular_functionlyase activity
C0016853molecular_functionisomerase activity
C0019242biological_processmethylglyoxal biosynthetic process
C0019563biological_processglycerol catabolic process
C0019682biological_processglyceraldehyde-3-phosphate metabolic process
C0031625molecular_functionubiquitin protein ligase binding
C0042803molecular_functionprotein homodimerization activity
C0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
C0061621biological_processcanonical glycolysis
D0004807molecular_functiontriose-phosphate isomerase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006006biological_processglucose metabolic process
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0008929molecular_functionmethylglyoxal synthase activity
D0016829molecular_functionlyase activity
D0016853molecular_functionisomerase activity
D0019242biological_processmethylglyoxal biosynthetic process
D0019563biological_processglycerol catabolic process
D0019682biological_processglyceraldehyde-3-phosphate metabolic process
D0031625molecular_functionubiquitin protein ligase binding
D0042803molecular_functionprotein homodimerization activity
D0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
D0061621biological_processcanonical glycolysis
Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
AALA163-GLY173

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Electrophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10127","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"4922541","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10127","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P60174","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"Deamidated asparagine","evidences":[{"source":"PubMed","id":"7574709","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P17751","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P60174","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P48500","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P17751","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17751","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P17751","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P17751","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P60174","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"UniProtKB","id":"P60174","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
ALYS13
AHIS95
AASN11
AGLU165
AGLY171

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
BLYS13
BHIS95
BASN11
BGLU165
BGLY171

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
CLYS13
CHIS95
CASN11
CGLU165
CGLY171

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
DLYS13
DHIS95
DASN11
DGLU165
DGLY171

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PDB entries from 2025-10-08

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