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2V0T

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
D0004807molecular_functiontriose-phosphate isomerase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0016853molecular_functionisomerase activity
D0019563biological_processglycerol catabolic process
D0020015cellular_componentglycosome
D0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
E0004807molecular_functiontriose-phosphate isomerase activity
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006094biological_processgluconeogenesis
E0006096biological_processglycolytic process
E0016853molecular_functionisomerase activity
E0019563biological_processglycerol catabolic process
E0020015cellular_componentglycosome
E0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
F0004807molecular_functiontriose-phosphate isomerase activity
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006094biological_processgluconeogenesis
F0006096biological_processglycolytic process
F0016853molecular_functionisomerase activity
F0019563biological_processglycerol catabolic process
F0020015cellular_componentglycosome
F0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
G0004807molecular_functiontriose-phosphate isomerase activity
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0006094biological_processgluconeogenesis
G0006096biological_processglycolytic process
G0016853molecular_functionisomerase activity
G0019563biological_processglycerol catabolic process
G0020015cellular_componentglycosome
G0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
H0004807molecular_functiontriose-phosphate isomerase activity
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0006094biological_processgluconeogenesis
H0006096biological_processglycolytic process
H0016853molecular_functionisomerase activity
H0019563biological_processglycerol catabolic process
H0020015cellular_componentglycosome
H0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A1251
ChainResidue
ASER213
AGLY234
AGLY235
AHOH2203
AHOH2204
AHOH2205
AHOH2206

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B1251
ChainResidue
BGLY235
BHOH2175
BHOH2194
BHOH2195
BHOH2196
BSER213
BGLY234

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C1251
ChainResidue
CTRP170
CSER213
CGLY234
CGLY235
CHOH2195
CHOH2196
CHOH2197
CHOH2198

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 D1251
ChainResidue
DSER213
DGLY234
DGLY235
DHOH2007
DHOH2205
DHOH2210
DHOH2211
DHOH2212
DHOH2213

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 E1251
ChainResidue
ESER213
EGLY234
EGLY235
EHOH2176
EHOH2191
EHOH2202

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 F1251
ChainResidue
FGLY234
FGLY235
FHOH2183
FHOH2184
FHOH2185
FHOH2186

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 G1251
ChainResidue
GGLY235
GHOH2007
GHOH2116
GHOH2126

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 H1251
ChainResidue
HSER213
HGLY234
HGLY235
HHOH2123
HHOH2132

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1252
ChainResidue
ATHR31
ASER32
AILE33
AHIS57
ALYS59

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 E1252
ChainResidue
ETHR31
ESER32
EILE33
EHIS57
EHOH2205
EHOH2206

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EPE C1252
ChainResidue
CLYS155
CHOH2200

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EPE D1252
ChainResidue
DASN29
DTHR31
DSER32
DILE33
DHIS57
DLYS59

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 Residues8
DetailsACT_SITE: Electrophile
ChainResidueDetails
AHIS95
BHIS95
CHIS95
DHIS95
EHIS95
FHIS95
GHIS95
HHIS95

site_idSWS_FT_FI2
Number of Residues8
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLU167
BGLU167
CGLU167
DGLU167
EGLU167
FGLU167
GGLU167
HGLU167

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AASN11
ELYS13
FASN11
FLYS13
GASN11
GLYS13
HASN11
HLYS13
ALYS13
BASN11
BLYS13
CASN11
CLYS13
DASN11
DLYS13
EASN11

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
ALYS13
AHIS95
AASN11
AGLU167

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

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
CLYS13
CHIS95
CASN11
CGLU167

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
DLYS13
DHIS95
DASN11
DGLU167
DGLY173

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
ELYS13
EHIS95
EASN11
EGLU167

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
FLYS13
FHIS95
FASN11
FGLU167

site_idCSA7
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
GLYS13
GHIS95
GASN11
GGLU167
GGLY173

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
HLYS13
HHIS95
HASN11
HGLU167

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PDB entries from 2024-05-01

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