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2Y62

Crystal structure of Leishmanial E65Q-TIM complexed with R-Glycidol phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0020015cellular_componentglycosome
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE G3P A 2250
ChainResidue
ALYS1013
AGLY1234
AGLY1235
AHOH3476
AHOH3477
AHOH3478
AHOH3479
AHIS1095
AGLU1167
AALA1171
AILE1172
AGLY1173
AGLY1212
ASER1213
ALEU1232

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 1GP A 2251
ChainResidue
ALYS1013
AHIS1095
AGLU1167
AALA1171
AILE1172
AGLY1173
AGLY1212
ASER1213
ALEU1232
AGLY1234
AGLY1235
AHOH3476
AHOH3477
AHOH3478
AHOH3479

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 2252
ChainResidue
ATHR1179
AGLU1181
AHOH3480
AHOH3481
AHOH3482

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GOL A 2253
ChainResidue
APHE1045
APHE1045
AASN1066
AASN1066
AGLY1076
AGLY1076
AGLU1077
AGLU1077
AARG1098
AHOH3257
AHOH3258
AHOH3483
AHOH3483
AHOH3484
AHOH3484

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
AALA1165-GLY1175

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Electrophile
ChainResidueDetails
AHIS1095

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU1167

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASN1011
ALYS1013

222624

PDB entries from 2024-07-17

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