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4HHP

Crystal structure of triosephosphate isomerase from trypanosoma cruzi, mutant e105d

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0020015cellular_componentglycosome
B0004807molecular_functiontriose-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0020015cellular_componentglycosome
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
ALYS157
ASER214
AGLY235
AGLY236
AHOH538

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
AHOH436
BMET51
BALA54
BHOH556

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BLYS157
BGLY235
BGLY236
BHOH426
BHOH433
BHOH442
BHOH634

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
AALA166-GLY176

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Electrophile => ECO:0000250
ChainResidueDetails
AHIS96
BHIS96

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AGLU168
BGLU168

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN12
ALYS14
BASN12
BLYS14

223166

PDB entries from 2024-07-31

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