Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6TGV

Crystal structure of Mycobacterium smegmatis CoaBC in complex with CTP and FMN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004632	molecular_function	phosphopantothenate--cysteine ligase activity
A	0004633	molecular_function	phosphopantothenoylcysteine decarboxylase activity
A	0010181	molecular_function	FMN binding
A	0015937	biological_process	coenzyme A biosynthetic process
A	0015941	biological_process	pantothenate catabolic process
A	0016829	molecular_function	lyase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0016874	molecular_function	ligase activity
A	0046872	molecular_function	metal ion binding
A	0071513	cellular_component	phosphopantothenoylcysteine decarboxylase complex
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0004632	molecular_function	phosphopantothenate--cysteine ligase activity
B	0004633	molecular_function	phosphopantothenoylcysteine decarboxylase activity
B	0010181	molecular_function	FMN binding
B	0015937	biological_process	coenzyme A biosynthetic process
B	0015941	biological_process	pantothenate catabolic process
B	0016829	molecular_function	lyase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0016874	molecular_function	ligase activity
B	0046872	molecular_function	metal ion binding
B	0071513	cellular_component	phosphopantothenoylcysteine decarboxylase complex
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0004632	molecular_function	phosphopantothenate--cysteine ligase activity
C	0004633	molecular_function	phosphopantothenoylcysteine decarboxylase activity
C	0010181	molecular_function	FMN binding
C	0015937	biological_process	coenzyme A biosynthetic process
C	0015941	biological_process	pantothenate catabolic process
C	0016829	molecular_function	lyase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0016874	molecular_function	ligase activity
C	0046872	molecular_function	metal ion binding
C	0071513	cellular_component	phosphopantothenoylcysteine decarboxylase complex
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0004632	molecular_function	phosphopantothenate--cysteine ligase activity
D	0004633	molecular_function	phosphopantothenoylcysteine decarboxylase activity
D	0010181	molecular_function	FMN binding
D	0015937	biological_process	coenzyme A biosynthetic process
D	0015941	biological_process	pantothenate catabolic process
D	0016829	molecular_function	lyase activity
D	0016831	molecular_function	carboxy-lyase activity
D	0016874	molecular_function	ligase activity
D	0046872	molecular_function	metal ion binding
D	0071513	cellular_component	phosphopantothenoylcysteine decarboxylase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue CTP A 501

Chain	Residue
A	MET275
A	ALA334
A	LYS350
A	MG505
A	ALA277
A	VAL279
A	ASP281
A	ASP309
A	VAL310
A	LEU311
A	PHE332
A	ALA333

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 502

Chain	Residue
A	LEU43
A	GLY47
A	ALA48
A	HOH602

site_id	AC3
Number of Residues	3
Details	binding site for residue EDO A 503

Chain	Residue
A	LYS19
A	LEU163
A	FMN506

site_id	AC4
Number of Residues	6
Details	binding site for residue EDO A 504

Chain	Residue
A	GLY142
A	VAL144
A	ALA180
A	ASP181
A	ALA182
A	LEU183

site_id	AC5
Number of Residues	2
Details	binding site for residue MG A 505

Chain	Residue
A	ASP281
A	CTP501

site_id	AC6
Number of Residues	19
Details	binding site for residue FMN A 506

Chain	Residue
A	ALA12
A	GLY13
A	ILE15
A	THR39
A	SER41
A	PHE45
A	VAL63
A	PHE64
A	HIS72
A	THR88
A	ALA89
A	ASP90
A	LEU91
A	ALA100
A	ASP101
A	ALA120
A	MET121
A	EDO503
B	ALA53

site_id	AC7
Number of Residues	11
Details	binding site for residue CTP B 501

Chain	Residue
B	MET275
B	ALA277
B	VAL279
B	ALA280
B	ASP308
B	ASP309
B	VAL310
B	LEU311
B	PHE332
B	ALA333
B	ALA334

site_id	AC8
Number of Residues	4
Details	binding site for residue EDO B 502

Chain	Residue
B	ARG6
B	ILE7
B	SER33
B	ARG35

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO B 503

Chain	Residue
B	ALA16
B	LYS19
B	ARG162
B	LEU163

site_id	AD1
Number of Residues	17
Details	binding site for residue FMN B 504

Chain	Residue
B	ALA12
B	GLY13
B	GLY14
B	ILE15
B	THR39
B	SER41
B	PHE45
B	THR88
B	ALA89
B	LEU91
B	ALA120
B	MET121
B	HOH602
D	VAL63
D	PHE64
D	ALA100
D	ASP101

site_id	AD2
Number of Residues	10
Details	binding site for residue CTP C 501

Chain	Residue
C	MET275
C	ALA277
C	VAL279
C	ALA280
C	ASP308
C	ASP309
C	VAL310
C	LEU311
C	PHE332
C	ALA334

site_id	AD3
Number of Residues	6
Details	binding site for residue EDO C 502

Chain	Residue
C	VAL144
C	ALA180
C	ASP181
C	ALA182
C	LEU183
C	PRO184

site_id	AD4
Number of Residues	20
Details	binding site for residue FMN C 503

Chain	Residue
B	PHE64
B	VAL67
B	HIS72
B	ALA100
C	ALA12
C	GLY13
C	GLY14
C	ILE15
C	THR39
C	SER41
C	PHE45
C	THR88
C	ALA89
C	ASP90
C	LEU91
C	ALA120
C	MET121
C	HOH601
C	HOH604
B	VAL63

site_id	AD5
Number of Residues	10
Details	binding site for residue CTP D 501

Chain	Residue
D	MET275
D	ALA277
D	VAL279
D	ASP281
D	ASP308
D	VAL310
D	LEU311
D	GLY331
D	PHE332
D	ALA333

site_id	AD6
Number of Residues	4
Details	binding site for residue EDO D 502

Chain	Residue
D	GLU147
D	ALA226
D	GLY229
D	ALA230

site_id	AD7
Number of Residues	18
Details	binding site for residue FMN D 503

Chain	Residue
C	VAL63
C	PHE64
C	HIS72
C	ALA100
D	ALA12
D	GLY13
D	GLY14
D	ILE15
D	THR39
D	SER41
D	PHE45
D	THR88
D	ALA89
D	ASP90
D	ARG94
D	ALA120
D	MET121
D	HOH602

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33420031","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2014","submissionDatabase":"PDB data bank","title":"Crystal structure of the C-terminal CTP-binding domain of a phosphopantothenoylcysteine decarboxylase/phosphopantothenate-cysteine ligase with bound CTP from Mycobacterium smegmatis.","authors":["Dranow D.M.","Abendroth J.","Wernimont A.K.","Edwards T.E.","Lorimer D."]}},{"source":"PDB","id":"4QJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6THC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02225","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33420031","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2014","submissionDatabase":"PDB data bank","title":"Crystal structure of the C-terminal CTP-binding domain of a phosphopantothenoylcysteine decarboxylase/phosphopantothenate-cysteine ligase with bound CTP from Mycobacterium smegmatis.","authors":["Dranow D.M.","Abendroth J.","Wernimont A.K.","Edwards T.E.","Lorimer D."]}},{"source":"PDB","id":"4QJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TH2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02225","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33420031","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2014","submissionDatabase":"PDB data bank","title":"Crystal structure of the C-terminal CTP-binding domain of a phosphopantothenoylcysteine decarboxylase/phosphopantothenate-cysteine ligase with bound CTP from Mycobacterium smegmatis.","authors":["Dranow D.M.","Abendroth J.","Wernimont A.K.","Edwards T.E.","Lorimer D."]}},{"source":"PDB","id":"4QJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6THC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02225","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33420031","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2014","submissionDatabase":"PDB data bank","title":"Crystal structure of the C-terminal CTP-binding domain of a phosphopantothenoylcysteine decarboxylase/phosphopantothenate-cysteine ligase with bound CTP from Mycobacterium smegmatis.","authors":["Dranow D.M.","Abendroth J.","Wernimont A.K.","Edwards T.E.","Lorimer D."]}},{"source":"PDB","id":"4QJI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6THC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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