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3RIM

Crystal structure of mycobacterium tuberculosis Transketolase (Rv1449c)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004802molecular_functiontransketolase activity
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006098biological_processpentose-phosphate shunt
A0009274cellular_componentpeptidoglycan-based cell wall
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004802molecular_functiontransketolase activity
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006098biological_processpentose-phosphate shunt
B0009274cellular_componentpeptidoglycan-based cell wall
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0004802molecular_functiontransketolase activity
C0005576cellular_componentextracellular region
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006098biological_processpentose-phosphate shunt
C0009274cellular_componentpeptidoglycan-based cell wall
C0016740molecular_functiontransferase activity
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0004802molecular_functiontransketolase activity
D0005576cellular_componentextracellular region
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006098biological_processpentose-phosphate shunt
D0009274cellular_componentpeptidoglycan-based cell wall
D0016740molecular_functiontransferase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1001
ChainResidue
AASP177
AASN207
AILE209
AHOH779
ATPP1002

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE TPP A 1002
ChainResidue
ASER176
AASP177
AGLY178
AGLU182
AASN207
AILE209
ASER210
AILE211
AHIS283
AHOH779
AMG1001
CASP401
CGLU441
CPHE467
CTYR470
CHIS503
CHOH748
ATHR48
AHIS85
AGLY133
ALEU135

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1001
ChainResidue
BASP177
BASN207
BILE209
BHOH819
BTPP1002

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TPP B 1002
ChainResidue
BTHR48
BHIS85
BGLY133
BLEU135
BSER176
BASP177
BGLY178
BGLU182
BASN207
BILE209
BSER210
BILE211
BILE269
BHIS283
BHOH819
BMG1001
DASP401
DGLU441
DPHE467
DTYR470
DHIS503
DHOH811

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 701
ChainResidue
BILE7
BSER8
BALA9

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 702
ChainResidue
BCYS220
DTYR230
DGLY231

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 1001
ChainResidue
CASP177
CASN207
CILE209
CHOH760
CTPP1002

site_idAC8
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TPP C 1002
ChainResidue
AASP401
AGLU441
APHE467
ATYR470
AHIS503
CTHR48
CHIS85
CGLY133
CPRO134
CLEU135
CSER176
CASP177
CGLY178
CGLU182
CASN207
CILE209
CSER210
CILE269
CHIS283
CHOH747
CHOH760
CMG1001

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL C 701
ChainResidue
CTRP430
CTYR431

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL C 702
ChainResidue
BHIS15
BHOH830
CARG123

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 1001
ChainResidue
DASP177
DASN207
DILE209
DHOH838
DTPP1002

site_idBC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE TPP D 1002
ChainResidue
BPHE467
BTYR470
BHIS503
DTHR48
DHIS85
DGLY133
DLEU135
DSER176
DASP177
DGLY178
DGLU182
DASN207
DILE209
DSER210
DILE269
DHIS283
DHOH738
DHOH838
DHOH840
DMG1001
BASP401
BVAL439
BGLU441

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL D 701
ChainResidue
DARG378
DSER405
DHIS491
DARG552

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL D 702
ChainResidue
DALA403
DASN407
DTHR409
DTYR426

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL D 703
ChainResidue
BARG351
BLYS356
DASP17
DTYR18

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL D 704
ChainResidue
DPHE122
DVAL452
DASP484

Functional Information from PROSITE/UniProt
site_idPS00801
Number of Residues21
DetailsTRANSKETOLASE_1 Transketolase signature 1. RvlaADavqkvgNGHPGtaMS
ChainResidueDetails
AARG31-SER51

site_idPS00802
Number of Residues17
DetailsTRANSKETOLASE_2 Transketolase signature 2. GEDGPTHqPIEhlSalR
ChainResidueDetails
AGLY497-ARG513

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AGLU441
BGLU441
CGLU441
DGLU441

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS45
BHIS491
BASP499
BARG552
CHIS45
CARG378
CSER405
CHIS491
CASP499
CARG552
DHIS45
AARG378
DARG378
DSER405
DHIS491
DASP499
DARG552
ASER405
AHIS491
AASP499
AARG552
BHIS45
BARG378
BSER405

site_idSWS_FT_FI3
Number of Residues32
DetailsBINDING:
ChainResidueDetails
ATHR48
BHIS85
BGLY133
BLEU135
BGLY178
BASN207
BHIS283
BPHE467
CTHR48
CHIS85
CGLY133
AHIS85
CLEU135
CGLY178
CASN207
CHIS283
CPHE467
DTHR48
DHIS85
DGLY133
DLEU135
DGLY178
AGLY133
DASN207
DHIS283
DPHE467
ALEU135
AGLY178
AASN207
AHIS283
APHE467
BTHR48

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:22645655
ChainResidueDetails
AASP177
AILE209
BASP177
BILE209
CASP177
CILE209
DASP177
DILE209

site_idSWS_FT_FI5
Number of Residues8
DetailsSITE: Important for catalytic activity => ECO:0000250
ChainResidueDetails
AHIS45
AHIS283
BHIS45
BHIS283
CHIS45
CHIS283
DHIS45
DHIS283

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609
ChainResidueDetails
ATHR2
BTHR2
CTHR2
DTHR2

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PDB entries from 2024-11-06

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