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6OOG

Crystal structure of triosephosphate isomerase from Taenia Solium in complex with 2PG

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
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue PGA A 301
ChainResidue
ALYS12
AGLY234
AGLY235
AHOH405
AHOH418
AHOH421
AHOH445
AHOH451
AHIS94
AGLU167
AALA171
AILE172
AGLY173
AGLY212
ASER213
ALEU232

site_idAC2
Number of Residues5
Detailsbinding site for residue NA A 302
ChainResidue
AGLN51
AASP52
AALA54
AHOH540
AHOH557

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
AALA165-GLY175

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Electrophile => ECO:0000250
ChainResidueDetails
AHIS94

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AGLU167

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN10
ALYS12

221051

PDB entries from 2024-06-12

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