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4POC

Structure of Triosephosphate Isomerase Wild Type human enzyme.

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 301
ChainResidue
AALA221
AGLN223
AVAL226
AHOH519

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 302
ChainResidue
BHOH444
AALA169
AGLY171
ATHR172
AGLY173
ALYS174

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 303
ChainResidue
AASN71
ATHR175
AHOH557

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PO4 B 301
ChainResidue
BLYS13
BALA169
BILE170
BGLY171
BGLY210
BSER211
BGLY232
BGLY233
BBR303
BHOH409
BHOH411
BHOH477
BHOH481

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K B 302
ChainResidue
BALA221
BGLN223
BVAL226
BHOH440
BHOH462
BHOH493
BHOH503

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BR B 303
ChainResidue
BASN11
BHIS95
BGLU165
BPO4301

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 Residues2
DetailsACT_SITE: Electrophile => ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000269|PubMed:8061610
ChainResidueDetails
ALYS58
BLYS58

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000269|PubMed:8061610
ChainResidueDetails
AGLY128
BGLY128

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
AALA30
AGLY171
BALA30
BGLY171

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
BALA42
AALA42

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48500
ChainResidueDetails
BLYS68
BVAL160
ALYS68
AVAL160

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
AGLN111
BGLN111

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
BALA118
BASP156
AALA118
AASP156

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
ALEU121
BLEU121

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
BGLU135
AGLU135

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ALYS174
BLYS174

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
AALA176
BALA176

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
AHIS185
BHIS185

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
AVAL200
BVAL200

site_idSWS_FT_FI14
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211
ChainResidueDetails
AGLU104
BGLU104

221051

PDB entries from 2024-06-12

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