Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6CVF

Crystal structure of Mycobacterium tuberculosis dethiobiotin synthetase in complex with cytidine diphosphate

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	23
Details	binding site for residue CDP A 301

Chain	Residue
A	GLY12
A	PRO197
A	GLY199
A	ALA200
A	ALA201
A	MG302
A	HOH406
A	HOH419
A	HOH450
A	HOH480
A	HOH483
A	VAL13
A	HOH532
A	HOH534
A	HOH542
A	HOH547
A	GLY14
A	LYS15
A	THR16
A	VAL17
A	GLU108
A	GLY169
A	LEU196

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 302

Chain	Residue
A	THR16
A	ASP49
A	GLU108
A	CDP301
A	HOH419
A	HOH547

site_id	AC3
Number of Residues	20
Details	binding site for residue CDP B 301

Chain	Residue
B	GLY12
B	VAL13
B	GLY14
B	LYS15
B	THR16
B	VAL17
B	GLU108
B	GLY169
B	LEU196
B	PRO197
B	GLY199
B	ALA200
B	ALA201
B	HOH405
B	HOH427
B	HOH436
B	HOH445
B	HOH515
B	HOH535
B	HOH537

site_id	AC4
Number of Residues	21
Details	binding site for residue CDP C 301

Chain	Residue
C	GLY12
C	VAL13
C	GLY14
C	LYS15
C	THR16
C	VAL17
C	GLU108
C	GLY169
C	SER170
C	LEU196
C	PRO197
C	GLY199
C	ALA200
C	ALA201
C	MG302
C	HOH427
C	HOH430
C	HOH431
C	HOH441
C	HOH480
C	HOH519

site_id	AC5
Number of Residues	7
Details	binding site for residue MG C 302

Chain	Residue
C	THR16
C	LYS37
C	ASP49
C	GLU108
C	CDP301
C	HOH480
C	HOH519

site_id	AC6
Number of Residues	19
Details	binding site for residue CDP D 301

Chain	Residue
D	GLY12
D	VAL13
D	GLY14
D	LYS15
D	THR16
D	VAL17
D	GLU108
D	GLY169
D	LEU196
D	PRO197
D	GLY199
D	ALA200
D	ALA201
D	MG302
D	HOH404
D	HOH415
D	HOH427
D	HOH429
D	HOH491

site_id	AC7
Number of Residues	7
Details	binding site for residue MG D 302

Chain	Residue
D	GLU108
D	CDP301
D	HOH415
D	HOH427
D	THR16
D	LYS37
D	ASP49

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00336

Chain	Residue	Details
A	LYS37
B	LYS37
C	LYS37
D	LYS37

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:25801336, ECO:0000269\|PubMed:30289406, ECO:0000269\|DOI:10.1021/acscatal.8b03475, ECO:0007744\|PDB:4WOP, ECO:0007744\|PDB:6CVE, ECO:0007744\|PDB:6CVF, ECO:0007744\|PDB:6E05, ECO:0007744\|PDB:6E06

Chain	Residue	Details
A	THR11
A	PRO197
B	THR11
B	PRO197
C	THR11
C	PRO197
D	THR11
D	PRO197

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00336, ECO:0000269\|PubMed:20565114, ECO:0000269\|PubMed:30289406, ECO:0000269\|DOI:10.1021/acscatal.8b03475, ECO:0007744\|PDB:3FPA, ECO:0007744\|PDB:6CVE, ECO:0007744\|PDB:6CVF, ECO:0007744\|PDB:6CVV, ECO:0007744\|PDB:6CZB, ECO:0007744\|PDB:6CZC, ECO:0007744\|PDB:6CZD, ECO:0007744\|PDB:6CZE, ECO:0007744\|PDB:6E05, ECO:0007744\|PDB:6E06

Chain	Residue	Details
A	THR16
D	THR16
D	ASP49
D	GLU108
A	ASP49
A	GLU108
B	THR16
B	ASP49
B	GLU108
C	THR16
C	ASP49
C	GLU108

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:20565114, ECO:0000269\|DOI:10.1021/acscatal.8b03475, ECO:0007744\|PDB:3FMF, ECO:0007744\|PDB:3FMI, ECO:0007744\|PDB:6CVE

Chain	Residue	Details
A	LYS37
B	LYS37
C	LYS37
D	LYS37

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00336

Chain	Residue	Details
A	THR41
B	THR41
C	THR41
D	THR41

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:20565114, ECO:0000269\|DOI:10.1021/acscatal.8b03475, ECO:0007744\|PDB:3FMF, ECO:0007744\|PDB:3FMI, ECO:0007744\|PDB:3FPA, ECO:0007744\|PDB:6CVE

Chain	Residue	Details
A	GLY144
B	GLY144
C	GLY144
D	GLY144

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:30289406, ECO:0000269\|DOI:10.1021/acscatal.8b03475, ECO:0007744\|PDB:6CVE, ECO:0007744\|PDB:6CVF, ECO:0007744\|PDB:6CVU, ECO:0007744\|PDB:6E05, ECO:0007744\|PDB:6E06

Chain	Residue	Details
A	GLY169
B	GLY169
C	GLY169
D	GLY169

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