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2V2C

The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A1251
ChainResidue
AARG134
ALYS156
AGLN182
AHOH2451
AHOH2452
AHOH2453
AHOH2454

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A1252
ChainResidue
AASN34
AHIS35
ALYS247
AGLN250
AHOH2455
AHOH2456
AHOH2457
ASER32
AILE33

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A1253
ChainResidue
ASER2
ALYS3
AHOH2458
AHOH2459

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PGA A1254
ChainResidue
AASN11
ALYS13
AHIS95
AGLU167
AALA171
AILE172
AGLY173
AGLY212
ASER213
ALEU232
AGLY234
AGLY235
AHOH2397
AHOH2460
AHOH2461
AHOH2462

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
ChainResidueDetails
AHIS95

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU167

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASN11
ALYS13

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
ALYS13
AHIS95
AASN11
AGLU167
AGLY173

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PDB entries from 2024-07-17

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