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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6CZE

Crystal structure of Mycobacterium tuberculosis dethiobiotin synthetase in complex with inosine triphosphate (ITP) - promiscuous binding mode with disordered nucleoside

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 Residues19
Detailsbinding site for residue ITT A 301
ChainResidue
ATHR11
AGLU52
AGLU108
AMG302
AHOH405
AHOH406
AHOH408
AHOH410
AHOH427
AHOH491
AHOH553
AGLY12
AVAL13
AGLY14
ALYS15
ATHR16
ALYS37
AARG45
AASP49
site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 302
ChainResidue
ATHR16
AASP49
AGLU108
AITT301
AHOH434
site_idAC3
Number of Residues21
Detailsbinding site for residue ITT B 301
ChainResidue
BGLY12
BVAL13
BGLY14
BLYS15
BTHR16
BLYS37
BARG45
BASP49
BGLU108
BGLY111
BMG302
BHOH405
BHOH409
BHOH411
BHOH418
BHOH423
BHOH441
BHOH458
BHOH482
BHOH494
BHOH514
site_idAC4
Number of Residues5
Detailsbinding site for residue MG B 302
ChainResidue
BTHR16
BASP49
BGLU108
BITT301
BHOH423
site_idAC5
Number of Residues21
Detailsbinding site for residue ITT C 301
ChainResidue
CGLY12
CVAL13
CGLY14
CLYS15
CTHR16
CVAL17
CLYS37
CASP49
CGLU108
CGLY169
CMG302
CHOH404
CHOH407
CHOH412
CHOH417
CHOH435
CHOH461
CHOH466
CHOH472
CHOH490
CHOH491
site_idAC6
Number of Residues5
Detailsbinding site for residue MG C 302
ChainResidue
CTHR16
CASP49
CGLU108
CITT301
CHOH417
site_idAC7
Number of Residues18
Detailsbinding site for residue ITT D 301
ChainResidue
DGLY12
DVAL13
DGLY14
DLYS15
DTHR16
DLYS37
DASP49
DGLU52
DGLU108
DGLY111
DMG302
DHOH401
DHOH407
DHOH410
DHOH412
DHOH414
DHOH426
DHOH490
site_idAC8
Number of Residues6
Detailsbinding site for residue MG D 302
ChainResidue
DHOH426
DTHR16
DLYS37
DASP49
DGLU108
DITT301
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

246704

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