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1TPH

1.8 ANGSTROMS CRYSTAL STRUCTURE OF WILD TYPE CHICKEN TRIOSEPHOSPHATE ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
10004807molecular_functiontriose-phosphate isomerase activity
10005737cellular_componentcytoplasm
10005829cellular_componentcytosol
10006094biological_processgluconeogenesis
10006096biological_processglycolytic process
10008929molecular_functionmethylglyoxal synthase activity
10016829molecular_functionlyase activity
10016853molecular_functionisomerase activity
10019242biological_processmethylglyoxal biosynthetic process
10019563biological_processglycerol catabolic process
10019682biological_processglyceraldehyde-3-phosphate metabolic process
10031625molecular_functionubiquitin protein ligase binding
10042803molecular_functionprotein homodimerization activity
10046166biological_processglyceraldehyde-3-phosphate biosynthetic process
10061621biological_processcanonical glycolysis
20004807molecular_functiontriose-phosphate isomerase activity
20005737cellular_componentcytoplasm
20005829cellular_componentcytosol
20006094biological_processgluconeogenesis
20006096biological_processglycolytic process
20008929molecular_functionmethylglyoxal synthase activity
20016829molecular_functionlyase activity
20016853molecular_functionisomerase activity
20019242biological_processmethylglyoxal biosynthetic process
20019563biological_processglycerol catabolic process
20019682biological_processglyceraldehyde-3-phosphate metabolic process
20031625molecular_functionubiquitin protein ligase binding
20042803molecular_functionprotein homodimerization activity
20046166biological_processglyceraldehyde-3-phosphate biosynthetic process
20061621biological_processcanonical glycolysis
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PGH 1 250
ChainResidue
1LYS13
1HIS95
1GLU165
1ALA169
1ILE170
1GLY171
1GLY210
1SER211
1LEU230
1GLY232
1GLY233
1HOH348
1HOH359
1HOH382
1HOH383
1ASN11

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PGH 2 250
ChainResidue
2ASN11
2LYS13
2HIS95
2GLU165
2ALA169
2ILE170
2GLY171
2GLY210
2SER211
2LEU230
2GLY232
2GLY233
2HOH405
2HOH415
2HOH417
2HOH518

site_idACT
Number of Residues4
Details
ChainResidue
1GLU165
1HIS95
1SER96
1LYS13

site_idBCT
Number of Residues4
Details
ChainResidue
2GLU165
2HIS95
2SER96
2LYS13

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
1ALA163-GLY173

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Electrophile","evidences":[{"source":"PubMed","id":"8130195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TPH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"8130195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TPH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8130195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TPH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 2204417, 2204418, 1569570, 8130195, 2005961
ChainResidueDetails
1LYS13
1HIS95
1ASN11
1GLU165
1GLY171

site_idCSA2
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 2204417, 2204418, 1569570, 8130195, 2005961
ChainResidueDetails
2LYS13
2HIS95
2ASN11
2GLU165
2GLY171

site_idMCSA1
Number of Residues7
DetailsM-CSA 324
ChainResidueDetails

site_idMCSA2
Number of Residues7
DetailsM-CSA 324
ChainResidueDetails

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PDB entries from 2025-12-24

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