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1HTI

CRYSTAL STRUCTURE OF RECOMBINANT HUMAN TRIOSEPHOSPHATE ISOMERASE AT 2.8 ANGSTROMS RESOLUTION. TRIOSEPHOSPHATE ISOMERASE RELATED HUMAN GENETIC DISORDERS AND COMPARISON WITH THE TRYPANOSOMAL 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 Residues12
DetailsBINDING SITE FOR RESIDUE PGA B 549
ChainResidue
BASN11
BLEU230
BGLY232
BGLY233
BLYS13
BHIS95
BGLU165
BALA169
BILE170
BGLY171
BGLY210
BSER211

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
ASER96
BSER96

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000269|PubMed:8061610
ChainResidueDetails
APRO166
BPRO166

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000269|PubMed:8061610
ChainResidueDetails
ATRP12
AMET14
BTRP12
BMET14

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
AMET14
APRO238
BMET14
BPRO238

site_idSWS_FT_FI5
Number of Residues2
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
ALEU21
BLEU21

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
ALYS68
AGLY209
BLYS68
BGLY209

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
APRO80
BPRO80

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48500
ChainResidueDetails
AASP106
AASP198
BASP106
BASP198

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
AVAL149
BVAL149

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
AASP156
ASER194
BASP156
BSER194

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
ALYS159
BLYS159

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17751
ChainResidueDetails
AGLY173
BGLY173

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
AVAL212
BVAL212

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
AGLY214
BGLY214

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
AGLN223
BGLN223

site_idSWS_FT_FI16
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211
ChainResidueDetails
AVAL142
BVAL142

218853

PDB entries from 2024-04-24

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