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2DP3

Crystal structure of a double mutant (C202A/A198V) of Triosephosphate isomerase from giardia lamblia

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0008929molecular_functionmethylglyoxal synthase activity
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 900
ChainResidue
ASER174
AHOH1001
AILE175
AGLY176
ASER216
AGLY237
AGLY238
AHOH923
AHOH925
AHOH943

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 901
ChainResidue
AARG135
AGLN185
AHOH1084

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 902
ChainResidue
ALYS195
AASN218
AALA239
ALYS242
AGLU244
AHOH1136
AHOH1137
AHOH1142

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 903
ChainResidue
AHIS24
AALA27
APRO243
AHOH987
AHOH1070
AHOH1151
AHOH1176

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWSIGTG
ChainResidueDetails
AALA168-GLY178

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Electrophile => ECO:0000255|PROSITE-ProRule:PRU10127
ChainResidueDetails
AHIS96

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127
ChainResidueDetails
AGLU170

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10127
ChainResidueDetails
AASN11
ALYS13

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
ALYS13
AGLU170
AHIS96
AASN11
AGLY176

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PDB entries from 2024-07-17

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