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5EYW

Crystal structure of Litopenaeus vannamei triosephosphate isomerase complexed with 2-Phosphoglycolic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
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
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 Residues16
Detailsbinding site for residue PGA A 301
ChainResidue
AASN12
AGLY233
AGLY234
AHOH474
AHOH475
AHOH480
AHOH498
AHOH544
ALYS14
AHIS96
AGLU166
AALA170
AILE171
AGLY172
ASER212
ALEU231

site_idAC2
Number of Residues16
Detailsbinding site for residue PGA B 301
ChainResidue
BASN12
BLYS14
BHIS96
BGLU166
BALA170
BILE171
BGLY172
BGLY211
BSER212
BLEU231
BGLY233
BGLY234
BHOH432
BHOH481
BHOH485
BHOH533

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

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PDB entries from 2024-07-17

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