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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7L1J

Mycobacterium tuberculosis dethiobiotin synthetase in complex with Tetrazole 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004141molecular_functiondethiobiotin synthase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009102biological_processbiotin biosynthetic process
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004141molecular_functiondethiobiotin synthase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009102biological_processbiotin biosynthetic process
B0016874molecular_functionligase activity
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0004141molecular_functiondethiobiotin synthase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0009102biological_processbiotin biosynthetic process
C0016874molecular_functionligase activity
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0004141molecular_functiondethiobiotin synthase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0009102biological_processbiotin biosynthetic process
D0016874molecular_functionligase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue XES A 301
ChainResidue
ATHR11
AVAL115
ASO4303
AHOH413
AHOH482
AHOH515
BLEU143
BGLY144
BTHR145
BLEU146
BASN147
ALYS15
BHOH451
ALYS37
AGLN40
ATHR41
AASP47
AASP49
AALA110
AGLY111
site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 302
ChainResidue
ATHR140
AASP142
ALEU143
AGLY144
ATHR145
AHIS148
AHOH414
AHOH432
site_idAC3
Number of Residues10
Detailsbinding site for residue SO4 A 303
ChainResidue
AGLY12
AVAL13
AGLY14
ALYS15
ATHR16
AXES301
AHOH413
AHOH440
AHOH498
AHOH563
site_idAC4
Number of Residues22
Detailsbinding site for residue XES B 301
ChainResidue
ALEU143
AGLY144
ATHR145
ALEU146
AASN147
AHOH449
BTHR11
BLYS15
BLYS37
BGLN40
BTHR41
BASP47
BASP49
BALA110
BGLY111
BVAL115
BSO4303
BHOH418
BHOH474
BHOH484
BHOH496
BHOH502
site_idAC5
Number of Residues8
Detailsbinding site for residue GOL B 302
ChainResidue
BTHR140
BASP142
BLEU143
BGLY144
BTHR145
BHIS148
BHOH432
BHOH559
site_idAC6
Number of Residues10
Detailsbinding site for residue SO4 B 303
ChainResidue
BGLY12
BVAL13
BGLY14
BLYS15
BTHR16
BXES301
BHOH410
BHOH418
BHOH496
BHOH552
site_idAC7
Number of Residues24
Detailsbinding site for residue XES C 301
ChainResidue
DTHR145
DLEU146
DASN147
CTHR11
CLYS15
CTHR16
CLYS37
CGLN40
CTHR41
CARG45
CASP49
CPRO71
CALA73
CPRO74
CALA110
CGLY111
CVAL115
CSO4303
CHOH403
CHOH472
CHOH491
CHOH503
DLEU143
DGLY144
site_idAC8
Number of Residues8
Detailsbinding site for residue GOL C 302
ChainResidue
CTHR140
CASP142
CLEU143
CGLY144
CTHR145
CHIS148
CHOH429
CHOH576
site_idAC9
Number of Residues10
Detailsbinding site for residue SO4 C 303
ChainResidue
CGLY12
CVAL13
CGLY14
CLYS15
CTHR16
CXES301
CHOH403
CHOH432
CHOH473
CHOH556
site_idAD1
Number of Residues6
Detailsbinding site for residue SO4 C 304
ChainResidue
BARG193
CHIS-1
CGLY0
CPRO101
CHOH525
CHOH529
site_idAD2
Number of Residues23
Detailsbinding site for residue XES D 301
ChainResidue
CLEU143
CGLY144
CTHR145
CLEU146
CASN147
CHOH444
DTHR11
DLYS15
DLYS37
DGLN40
DTHR41
DARG45
DASP47
DASP49
DALA73
DALA110
DGLY111
DVAL115
DSO4303
DHOH430
DHOH439
DHOH464
DHOH489
site_idAD3
Number of Residues6
Detailsbinding site for residue GOL D 302
ChainResidue
DTHR140
DASP142
DGLY144
DTHR145
DHIS148
DHOH425
site_idAD4
Number of Residues9
Detailsbinding site for residue SO4 D 303
ChainResidue
DGLY12
DVAL13
DGLY14
DLYS15
DTHR16
DXES301
DHOH430
DHOH439
DHOH508
site_idAD5
Number of Residues2
Detailsbinding site for residue SO4 D 304
ChainResidue
AARG45
DARG93
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00336","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25801336","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30289406","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2018","firstPage":"10774","lastPage":"10783","volume":"8","journal":"ACS Catal.","title":"Mycobacterium tuberculosis Dethiobiotin Synthetase Facilitates Nucleoside Triphosphate Promiscuity through Alternate Binding Modes.","authors":["Thompson A.P.","Salaemae W.","Pederick J.L.","Abell A.D.","Booker G.W.","Bruning J.B.","Polyak S.W."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.8b03475"}]}},{"source":"PDB","id":"4WOP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6E05","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6E06","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00336","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20565114","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30289406","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2018","firstPage":"10774","lastPage":"10783","volume":"8","journal":"ACS Catal.","title":"Mycobacterium tuberculosis Dethiobiotin Synthetase Facilitates Nucleoside Triphosphate Promiscuity through Alternate Binding Modes.","authors":["Thompson A.P.","Salaemae W.","Pederick J.L.","Abell A.D.","Booker G.W.","Bruning J.B.","Polyak S.W."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.8b03475"}]}},{"source":"PDB","id":"3FPA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CZB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CZC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CZD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CZE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6E05","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6E06","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20565114","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2018","firstPage":"10774","lastPage":"10783","volume":"8","journal":"ACS Catal.","title":"Mycobacterium tuberculosis Dethiobiotin Synthetase Facilitates Nucleoside Triphosphate Promiscuity through Alternate Binding Modes.","authors":["Thompson A.P.","Salaemae W.","Pederick J.L.","Abell A.D.","Booker G.W.","Bruning J.B.","Polyak S.W."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.8b03475"}]}},{"source":"PDB","id":"3FMF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FMI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CVE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00336","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20565114","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2018","firstPage":"10774","lastPage":"10783","volume":"8","journal":"ACS Catal.","title":"Mycobacterium tuberculosis Dethiobiotin Synthetase Facilitates Nucleoside Triphosphate Promiscuity through Alternate Binding Modes.","authors":["Thompson A.P.","Salaemae W.","Pederick J.L.","Abell A.D.","Booker G.W.","Bruning J.B.","Polyak S.W."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.8b03475"}]}},{"source":"PDB","id":"3FMF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FMI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FPA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CVE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30289406","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2018","firstPage":"10774","lastPage":"10783","volume":"8","journal":"ACS Catal.","title":"Mycobacterium tuberculosis Dethiobiotin Synthetase Facilitates Nucleoside Triphosphate Promiscuity through Alternate Binding Modes.","authors":["Thompson A.P.","Salaemae W.","Pederick J.L.","Abell A.D.","Booker G.W.","Bruning J.B.","Polyak S.W."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.8b03475"}]}},{"source":"PDB","id":"6CVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CVU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6E05","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6E06","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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