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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
DetailsACT_SITE: Electrophile => ECO:0000255|PROSITE-ProRule:PRU10127
ChainResidueDetails
ASER96
BSER96
CSER96
DSER96

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:4922541
ChainResidueDetails
APRO166
BPRO166
CPRO166
DPRO166

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10127
ChainResidueDetails
ATRP12
AMET14
BTRP12
BMET14
CTRP12
CMET14
DTRP12
DMET14

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P60174
ChainResidueDetails
AMET14
APRO238
BMET14
BPRO238
CMET14
CPRO238
DMET14
DPRO238

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: Deamidated asparagine => ECO:0000269|PubMed:7574709
ChainResidueDetails
AGLY16
AGLY72
BGLY16
BGLY72
CGLY16
CGLY72
DGLY16
DGLY72

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
ALYS68
AGLY209
BLYS68
BGLY209
CLYS68
CGLY209
DLYS68
DGLY209

site_idSWS_FT_FI7
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P60174
ChainResidueDetails
APRO80
DPRO80
DVAL212
DGLN223
AVAL212
AGLN223
BPRO80
BVAL212
BGLN223
CPRO80
CVAL212
CGLN223

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48500
ChainResidueDetails
AASP106
AASP198
BASP106
BASP198
CASP106
CASP198
DASP106
DASP198

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
AVAL149
BVAL149
CVAL149
DVAL149

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
AASP156
ASER194
BASP156
BSER194
CASP156
CSER194
DASP156
DSER194

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
ALYS159
BLYS159
CLYS159
DLYS159

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
AGLY173
BGLY173
CGLY173
DGLY173

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P60174
ChainResidueDetails
AGLY214
BGLY214
CGLY214
DGLY214

site_idSWS_FT_FI14
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250|UniProtKB:P60174
ChainResidueDetails
AVAL142
BVAL142
CVAL142
DVAL142

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 2024-07-24

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