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1BTM

TRIOSEPHOSPHATE ISOMERASE (TIM) COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0019563biological_processglycerol catabolic process
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0004807molecular_functiontriose-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0019563biological_processglycerol catabolic process
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PGA A 560
ChainResidue
AASN8
AGLY233
AGLY234
ALYS10
AHIS94
AGLU166
AALA170
AILE171
AGLY172
ASER212
ALEU231

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PGA B 570
ChainResidue
BASN8
BLYS10
BHIS94
BGLU166
BILE171
BGLY172
BGLY211
BSER212
BLEU231
BGLY233
BGLY234

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPIWAIGTG
ChainResidueDetails
AALA164-GLY174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Electrophile => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000305|PubMed:10383424, ECO:0000305|PubMed:8580851
ChainResidueDetails
AHIS94
BHIS94

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000305|PubMed:10383424
ChainResidueDetails
AGLU166
BGLU166

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:10383424, ECO:0000269|PubMed:8580851
ChainResidueDetails
AASN8
AGLY172
ASER212
AGLY233
BASN8
BGLY172
BSER212
BGLY233

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000255|HAMAP-Rule:MF_00147
ChainResidueDetails
ASER212
BSER212

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
AGLY172
AASN8
ALYS10
AGLU166
AHIS94

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
BGLY172
BASN8
BLYS10
BGLU166
BHIS94

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PDB entries from 2024-07-10

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