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3TAO

Structure of Mycobacterium tuberculosis triosephosphate isomerase bound to phosphoglycolohydroxamate

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 Residues17
DetailsBINDING SITE FOR RESIDUE PGH A 268
ChainResidue
AASN10
ASER218
ALEU237
AGLY239
AGLY240
AHOH278
AHOH317
AHOH338
AHOH414
ALYS12
AHIS100
AGLU172
AALA176
AILE177
AGLY178
AGLY216
AGLY217

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PGH A 269
ChainResidue
AILE21
AARG51
ASER52
ATHR55
AHOH286
AHOH400
AHOH400
AHOH756
AHOH756
BARG51
BTHR55

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

220113

PDB entries from 2024-05-22

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