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2VOM

Structural basis of human triosephosphate isomerase deficiency. Mutation E104D and correlation to solvent perturbation.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
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
A0070062cellular_componentextracellular exosome
B0004807molecular_functiontriose-phosphate isomerase activity
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
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
B0070062cellular_componentextracellular exosome
C0004807molecular_functiontriose-phosphate isomerase activity
C0005515molecular_functionprotein binding
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
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
C0070062cellular_componentextracellular exosome
D0004807molecular_functiontriose-phosphate isomerase activity
D0005515molecular_functionprotein binding
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
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
D0070062cellular_componentextracellular exosome
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, ECO:0000269|PubMed:8061610
ChainResidueDetails
AHIS95
BHIS95
CHIS95
DHIS95

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000269|PubMed:8061610
ChainResidueDetails
AGLU165
BGLU165
CGLU165
DGLU165

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000269|PubMed:8061610
ChainResidueDetails
AASN11
ALYS13
BASN11
BLYS13
CASN11
CLYS13
DASN11
DLYS13

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS13
ALYS237
BLYS13
BLYS237
CLYS13
CLYS237
DLYS13
DLYS237

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER20
BSER20
CSER20
DSER20

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
ATYR67
ATYR208
BTYR67
BTYR208
CTYR67
CTYR208
DTYR67
DTYR208

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER79
BSER79
CSER79
DSER79

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48500
ChainResidueDetails
ASER105
ASER197
BSER105
BSER197
CSER105
CSER197
DSER105
DSER197

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
ALYS148
BLYS148
CLYS148
DLYS148

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
ALYS155
ALYS193
BLYS155
BLYS193
CLYS155
CLYS193
DLYS155
DLYS193

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
ASER158
BSER158
CSER158
DSER158

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
ATHR172
BTHR172
CTHR172
DTHR172

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER211
BSER211
CSER211
DSER211

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR213
BTHR213
CTHR213
DTHR213

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER222
BSER222
CSER222
DSER222

site_idSWS_FT_FI16
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211
ChainResidueDetails
ALYS141
BLYS141
CLYS141
DLYS141

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 2024-07-17

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