Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WGF

Crystal structure of Mycobacterium tuberculosis C171Q KasA variant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0016746	molecular_function	acyltransferase activity
A	0019367	biological_process	fatty acid elongation, saturated fatty acid
A	0030497	biological_process	fatty acid elongation
A	0042802	molecular_function	identical protein binding
B	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0016746	molecular_function	acyltransferase activity
B	0019367	biological_process	fatty acid elongation, saturated fatty acid
B	0030497	biological_process	fatty acid elongation
B	0042802	molecular_function	identical protein binding
C	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0016746	molecular_function	acyltransferase activity
C	0019367	biological_process	fatty acid elongation, saturated fatty acid
C	0030497	biological_process	fatty acid elongation
C	0042802	molecular_function	identical protein binding
D	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0016746	molecular_function	acyltransferase activity
D	0019367	biological_process	fatty acid elongation, saturated fatty acid
D	0030497	biological_process	fatty acid elongation
D	0042802	molecular_function	identical protein binding
E	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0016746	molecular_function	acyltransferase activity
E	0019367	biological_process	fatty acid elongation, saturated fatty acid
E	0030497	biological_process	fatty acid elongation
E	0042802	molecular_function	identical protein binding
F	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0016746	molecular_function	acyltransferase activity
F	0019367	biological_process	fatty acid elongation, saturated fatty acid
F	0030497	biological_process	fatty acid elongation
F	0042802	molecular_function	identical protein binding
G	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0005886	cellular_component	plasma membrane
G	0016746	molecular_function	acyltransferase activity
G	0019367	biological_process	fatty acid elongation, saturated fatty acid
G	0030497	biological_process	fatty acid elongation
G	0042802	molecular_function	identical protein binding
H	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0005886	cellular_component	plasma membrane
H	0016746	molecular_function	acyltransferase activity
H	0019367	biological_process	fatty acid elongation, saturated fatty acid
H	0030497	biological_process	fatty acid elongation
H	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 1417

Chain	Residue
A	ASN309
A	ALA310
A	GLU354
A	ASN399
A	ASN400

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PG4 E 1417

Chain	Residue
E	LEU205
E	ALA209
F	VAL142

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PG4 A 1418

Chain	Residue
A	LEU205

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PG4 F 1417

Chain	Residue
F	GLY115

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PG4 C 1417

Chain	Residue
C	LEU205

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PG4 D 1417

Chain	Residue
D	GLY115
D	ALA119
D	PRO206

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PG4 B 1417

Chain	Residue
B	LEU116
B	GLU199
B	GLY200
B	PHE239
B	HIS345

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PG4 B 1418

Chain	Residue
B	GLU203

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG D 1418

Chain	Residue
D	LEU116
D	GLU199
D	PHE239
D	ILE347

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA D 1419

Chain	Residue
D	ASN309
D	ALA310
D	HIS311
D	GLU354
D	ASN399
D	ASN400

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA C 1418

Chain	Residue
C	ASN309
C	ALA310
C	HIS311
C	GLU354
C	ASN399
C	ASN400

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA B 1419

Chain	Residue
B	ASN309
B	ALA310
B	HIS311
B	GLU354
B	ASN399
B	ASN400

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA E 1418

Chain	Residue
E	ASN309
E	ALA310
E	HIS311
E	GLU354
E	ASN399
E	ASN400

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA H 1417

Chain	Residue
H	ASN309
H	ALA310
H	HIS311
H	GLU354
H	ASN399
H	ASN400

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA F 1418

Chain	Residue
F	ASN309
F	ALA310
F	HIS311
F	GLU354
F	ASN399
F	ASN400

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA G 1417

Chain	Residue
G	ASN309
G	ALA310
G	HIS311
G	GLU354
G	ASN399
G	ASN400

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3232
Details	Domain: {"description":"Ketosynthase family 3 (KS3)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19604480","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24108128","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24479625","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Active site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19604480","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24108128","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	24
Details	Site: {"description":"Interacts with the inhibitor thiolactomycin","evidences":[{"source":"PubMed","id":"19604480","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24108128","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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