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3GVG

Crystal structure of Triosephosphate isomerase from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0019563biological_processglycerol catabolic process
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0004807molecular_functiontriose-phosphate isomerase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0019563biological_processglycerol catabolic process
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 300
ChainResidue
AASN10
ALYS12
AHIS100
AGLU172
AGLY239
AHOH389
AHOH456
AHOH581

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 300
ChainResidue
BLYS12
BHIS100
BGLU172
BILE177
BGLY216
BGLY239
BGOL301
BHOH401
BASN10

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
BLYS12
BGLY239
BGLY240
BHOH281
BGOL300
BHOH375
BHOH407

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
ChainResidueDetails
AALA170-GLY180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Electrophile => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000305|PubMed:22120738, ECO:0000305|PubMed:25613812
ChainResidueDetails
AHIS100
BHIS100

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000305|PubMed:25613812
ChainResidueDetails
AGLU172
BGLU172

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:22120738, ECO:0000269|PubMed:25613812
ChainResidueDetails
AASN10
BASN10

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:22120738
ChainResidueDetails
AGLY178
ASER218
AGLY239
BGLY178
BSER218
BGLY239

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
AGLU172
AHIS100
AASN10
AGLY178
ALYS12

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1hti
ChainResidueDetails
BGLU172
BHIS100
BASN10
BGLY178
BLYS12

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PDB entries from 2024-07-24

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