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5ZFX

Crystal Structure of Triosephosphate isomerase from Opisthorchis viverrini

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
A0046872molecular_functionmetal ion binding
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
B0046872molecular_functionmetal ion binding
C0004807molecular_functiontriose-phosphate isomerase activity
C0005829cellular_componentcytosol
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016853molecular_functionisomerase activity
C0019563biological_processglycerol catabolic process
C0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
C0046872molecular_functionmetal ion binding
D0004807molecular_functiontriose-phosphate isomerase activity
D0005829cellular_componentcytosol
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0016853molecular_functionisomerase activity
D0019563biological_processglycerol catabolic process
D0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG B 301
ChainResidue
BGLU27
BHIS31
BHOH433
BHOH559
CHOH352

site_idAC2
Number of Residues6
Detailsbinding site for residue MG B 302
ChainResidue
BHOH643
BHOH649
BALA173
BTHR176
BLYS178
BHOH477

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
AALA167-GLY177

226707

PDB entries from 2024-10-30

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