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2V2H

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
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0019563biological_processglycerol catabolic process
A0020015cellular_componentglycosome
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0004807molecular_functiontriose-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0019563biological_processglycerol catabolic process
B0020015cellular_componentglycosome
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
C0004807molecular_functiontriose-phosphate isomerase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016853molecular_functionisomerase activity
C0019563biological_processglycerol catabolic process
C0020015cellular_componentglycosome
C0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PGA A1251
ChainResidue
AASN11
AGLY234
AGLY235
AHOH2253
AHOH2287
AHOH2288
AHOH2289
ALYS13
AHIS95
AGLU167
AALA171
AILE172
AGLY173
AGLY212
ASER213

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PGA B1251
ChainResidue
BASN11
BLYS13
BHIS95
BGLU167
BALA171
BILE172
BGLY173
BGLY212
BSER213
BGLY234
BGLY235
BHOH2246
BHOH2284
BHOH2285
BHOH2286

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PGA C1251
ChainResidue
CASN11
CLYS13
CHIS95
CGLU167
CALA171
CILE172
CGLY173
CGLY212
CSER213
CGLY234
CGLY235
CHOH2270
CHOH2271
CHOH2272
CHOH2273

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C1252
ChainResidue
BLYS52
BPHE86
CLEU131
CTRP170

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B1252
ChainResidue
ALYS52
APHE86
BLEU131
BTRP170

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A1252
ChainResidue
ALEU131
CLYS52
CPHE86

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 Residues3
DetailsACT_SITE: Electrophile
ChainResidueDetails
AHIS95
BHIS95
CHIS95

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU167
BGLU167
CGLU167

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASN11
ALYS13
BASN11
BLYS13
CASN11
CLYS13

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

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
BLYS13
BHIS95
BASN11
BGLU167
BGLY173

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
CLYS13
CHIS95
CASN11
CGLU167
CGLY173

225158

PDB entries from 2024-09-18

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