Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7JT5

Mycobacterium tuberculosis dethiobiotin synthetase in complex with fragment analogue 9

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0004141	molecular_function	dethiobiotin synthase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009102	biological_process	biotin biosynthetic process
A	0016874	molecular_function	ligase activity
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0004141	molecular_function	dethiobiotin synthase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0009102	biological_process	biotin biosynthetic process
B	0016874	molecular_function	ligase activity
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0004141	molecular_function	dethiobiotin synthase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0009102	biological_process	biotin biosynthetic process
C	0016874	molecular_function	ligase activity
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0004141	molecular_function	dethiobiotin synthase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0009102	biological_process	biotin biosynthetic process
D	0016874	molecular_function	ligase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue GOL A 401

Chain	Residue
A	THR140
A	ASP142
A	GLY144
A	THR145
A	HIS148
A	HOH525
B	SO4404

site_id	AC2
Number of Residues	22
Details	binding site for residue VJS A 402

Chain	Residue
A	LYS37
A	GLN40
A	THR41
A	ASP47
A	ASP49
A	ALA73
A	PRO74
A	ALA110
A	GLY111
A	VAL115
A	SO4403
A	HOH503
A	HOH507
A	HOH560
B	LEU143
B	GLY144
B	THR145
B	LEU146
B	ASN147
B	HOH526
A	THR11
A	LYS15

site_id	AC3
Number of Residues	10
Details	binding site for residue SO4 A 403

Chain	Residue
A	GLY12
A	VAL13
A	GLY14
A	LYS15
A	THR16
A	VJS402
A	SO4405
A	HOH503
A	HOH521
A	HOH571

site_id	AC4
Number of Residues	7
Details	binding site for residue SO4 A 404

Chain	Residue
A	GLY10
A	THR11
B	LEU143
B	GLY144
B	HIS148
B	GOL401
B	HOH528

site_id	AC5
Number of Residues	5
Details	binding site for residue SO4 A 405

Chain	Residue
A	GLY12
A	VAL13
A	GLY14
A	GLY169
A	SO4403

site_id	AC6
Number of Residues	8
Details	binding site for residue GOL B 401

Chain	Residue
A	SO4404
B	THR140
B	ASP142
B	GLY144
B	THR145
B	HIS148
B	SO4404
B	HOH503

site_id	AC7
Number of Residues	22
Details	binding site for residue VJS B 402

Chain	Residue
A	LEU143
A	GLY144
A	THR145
A	LEU146
A	ASN147
A	HOH514
B	THR11
B	LYS15
B	LYS37
B	GLN40
B	THR41
B	ASP49
B	ALA73
B	PRO74
B	ALA110
B	GLY111
B	VAL115
B	SO4403
B	HOH505
B	HOH527
B	HOH543
B	HOH574

site_id	AC8
Number of Residues	10
Details	binding site for residue SO4 B 403

Chain	Residue
B	GLY12
B	VAL13
B	GLY14
B	LYS15
B	THR16
B	VJS402
B	SO4405
B	HOH505
B	HOH542
B	HOH574

site_id	AC9
Number of Residues	7
Details	binding site for residue SO4 B 404

Chain	Residue
A	LEU143
A	HIS148
A	GOL401
A	HOH524
B	GLY10
B	THR11
B	GOL401

site_id	AD1
Number of Residues	5
Details	binding site for residue SO4 B 405

Chain	Residue
B	VAL17
B	SO4403
B	HOH542
B	HOH572
B	GLY14

site_id	AD2
Number of Residues	7
Details	binding site for residue GOL C 401

Chain	Residue
C	THR140
C	ASP142
C	GLY144
C	THR145
C	HIS148
C	HOH506
D	SO4404

site_id	AD3
Number of Residues	23
Details	binding site for residue VJS C 402

Chain	Residue
C	THR11
C	LYS15
C	LYS37
C	GLN40
C	THR41
C	ARG45
C	ASP49
C	ALA73
C	PRO74
C	ALA110
C	GLY111
C	VAL115
C	SO4403
C	HOH509
C	HOH513
C	HOH526
C	HOH541
C	HOH561
D	LEU143
D	GLY144
D	THR145
D	LEU146
D	ASN147

site_id	AD4
Number of Residues	9
Details	binding site for residue SO4 C 403

Chain	Residue
C	GLY12
C	VAL13
C	GLY14
C	LYS15
C	THR16
C	VJS402
C	HOH514
C	HOH526
C	HOH575

site_id	AD5
Number of Residues	7
Details	binding site for residue SO4 C 404

Chain	Residue
C	GLY10
C	THR11
C	HOH581
D	GLY144
D	HIS148
D	GOL401
D	HOH513

site_id	AD6
Number of Residues	5
Details	binding site for residue SO4 C 405

Chain	Residue
B	MET191
B	ARG193
B	TRP220
C	GLY0
C	PRO101

site_id	AD7
Number of Residues	8
Details	binding site for residue GOL D 401

Chain	Residue
C	SO4404
D	THR140
D	ASP142
D	GLY144
D	THR145
D	HIS148
D	SO4404
D	HOH509

site_id	AD8
Number of Residues	23
Details	binding site for residue VJS D 402

Chain	Residue
C	LEU143
C	GLY144
C	THR145
C	LEU146
C	ASN147
C	HOH523
D	THR11
D	LYS15
D	LYS37
D	GLN40
D	THR41
D	ASP49
D	MET72
D	ALA73
D	PRO74
D	ALA110
D	GLY111
D	VAL115
D	SO4403
D	HOH505
D	HOH507
D	HOH521
D	HOH551

site_id	AD9
Number of Residues	10
Details	binding site for residue SO4 D 403

Chain	Residue
D	GLY12
D	VAL13
D	GLY14
D	LYS15
D	THR16
D	VJS402
D	HOH505
D	HOH507
D	HOH525
D	HOH535

site_id	AE1
Number of Residues	9
Details	binding site for residue SO4 D 404

Chain	Residue
C	LEU143
C	GLY144
C	HIS148
C	GOL401
C	HOH528
D	GLY10
D	THR11
D	GOL401
D	HOH553

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00336","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	40
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00336","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding 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"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)