Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6TZV

Crystal Structure of the carboxyltransferase subunit of ACC (AccD6) in complex with inhibitor Phenyl-Cyclodiaone from Mycobacterium tuberculosis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003989	molecular_function	acetyl-CoA carboxylase activity
A	0004658	molecular_function	propionyl-CoA carboxylase activity
A	0005515	molecular_function	protein binding
A	0006633	biological_process	fatty acid biosynthetic process
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0009317	cellular_component	acetyl-CoA carboxylase complex
A	0016740	molecular_function	transferase activity
A	0016874	molecular_function	ligase activity
A	0019367	biological_process	fatty acid elongation, saturated fatty acid
B	0003989	molecular_function	acetyl-CoA carboxylase activity
B	0004658	molecular_function	propionyl-CoA carboxylase activity
B	0005515	molecular_function	protein binding
B	0006633	biological_process	fatty acid biosynthetic process
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0009317	cellular_component	acetyl-CoA carboxylase complex
B	0016740	molecular_function	transferase activity
B	0016874	molecular_function	ligase activity
B	0019367	biological_process	fatty acid elongation, saturated fatty acid
C	0003989	molecular_function	acetyl-CoA carboxylase activity
C	0004658	molecular_function	propionyl-CoA carboxylase activity
C	0005515	molecular_function	protein binding
C	0006633	biological_process	fatty acid biosynthetic process
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0009317	cellular_component	acetyl-CoA carboxylase complex
C	0016740	molecular_function	transferase activity
C	0016874	molecular_function	ligase activity
C	0019367	biological_process	fatty acid elongation, saturated fatty acid
D	0003989	molecular_function	acetyl-CoA carboxylase activity
D	0004658	molecular_function	propionyl-CoA carboxylase activity
D	0005515	molecular_function	protein binding
D	0006633	biological_process	fatty acid biosynthetic process
D	0009274	cellular_component	peptidoglycan-based cell wall
D	0009317	cellular_component	acetyl-CoA carboxylase complex
D	0016740	molecular_function	transferase activity
D	0016874	molecular_function	ligase activity
D	0019367	biological_process	fatty acid elongation, saturated fatty acid
E	0003989	molecular_function	acetyl-CoA carboxylase activity
E	0004658	molecular_function	propionyl-CoA carboxylase activity
E	0005515	molecular_function	protein binding
E	0006633	biological_process	fatty acid biosynthetic process
E	0009274	cellular_component	peptidoglycan-based cell wall
E	0009317	cellular_component	acetyl-CoA carboxylase complex
E	0016740	molecular_function	transferase activity
E	0016874	molecular_function	ligase activity
E	0019367	biological_process	fatty acid elongation, saturated fatty acid
F	0003989	molecular_function	acetyl-CoA carboxylase activity
F	0004658	molecular_function	propionyl-CoA carboxylase activity
F	0005515	molecular_function	protein binding
F	0006633	biological_process	fatty acid biosynthetic process
F	0009274	cellular_component	peptidoglycan-based cell wall
F	0009317	cellular_component	acetyl-CoA carboxylase complex
F	0016740	molecular_function	transferase activity
F	0016874	molecular_function	ligase activity
F	0019367	biological_process	fatty acid elongation, saturated fatty acid
G	0003989	molecular_function	acetyl-CoA carboxylase activity
G	0004658	molecular_function	propionyl-CoA carboxylase activity
G	0005515	molecular_function	protein binding
G	0006633	biological_process	fatty acid biosynthetic process
G	0009274	cellular_component	peptidoglycan-based cell wall
G	0009317	cellular_component	acetyl-CoA carboxylase complex
G	0016740	molecular_function	transferase activity
G	0016874	molecular_function	ligase activity
G	0019367	biological_process	fatty acid elongation, saturated fatty acid
H	0003989	molecular_function	acetyl-CoA carboxylase activity
H	0004658	molecular_function	propionyl-CoA carboxylase activity
H	0005515	molecular_function	protein binding
H	0006633	biological_process	fatty acid biosynthetic process
H	0009274	cellular_component	peptidoglycan-based cell wall
H	0009317	cellular_component	acetyl-CoA carboxylase complex
H	0016740	molecular_function	transferase activity
H	0016874	molecular_function	ligase activity
H	0019367	biological_process	fatty acid elongation, saturated fatty acid

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue PKP A 501

Chain	Residue
A	GLY98
B	LEU345
B	GLY366
B	ALA370
B	VAL391
A	ALA99
A	PHE115
A	GLY137
A	GLY138
A	TYR141
B	ALA300
B	TYR326
B	GLY341

site_id	AC2
Number of Residues	15
Details	binding site for residue PKP B 501

Chain	Residue
A	LEU295
A	ALA300
A	TYR326
A	GLY341
A	LEU345
A	GLY365
A	GLY366
A	ALA370
A	MET392
B	GLY98
B	ALA99
B	PHE115
B	GLY137
B	GLY138
B	TYR141

site_id	AC3
Number of Residues	13
Details	binding site for residue PKP C 501

Chain	Residue
C	GLY98
C	ALA99
C	PHE115
C	GLY137
C	GLY138
C	TYR141
D	ALA300
D	TYR326
D	GLY341
D	LEU345
D	GLY366
D	ALA370
D	VAL391

site_id	AC4
Number of Residues	14
Details	binding site for residue PKP D 501

Chain	Residue
C	ALA300
C	TYR326
C	GLY341
C	LEU345
C	GLY365
C	GLY366
C	ALA370
C	VAL391
D	GLY98
D	ALA99
D	PHE115
D	GLY137
D	GLY138
D	TYR141

site_id	AC5
Number of Residues	14
Details	binding site for residue PKP E 501

Chain	Residue
E	GLY98
E	ALA99
E	PHE115
E	GLY137
E	GLY138
E	TYR141
F	LEU295
F	ALA300
F	TYR326
F	GLY341
F	LEU345
F	GLY366
F	ALA370
F	VAL391

site_id	AC6
Number of Residues	15
Details	binding site for residue PKP F 501

Chain	Residue
E	LEU295
E	ALA300
E	TYR326
E	GLY341
E	LEU345
E	GLY365
E	GLY366
E	ALA370
E	MET392
F	GLY98
F	ALA99
F	PHE115
F	GLY137
F	GLY138
F	TYR141

site_id	AC7
Number of Residues	13
Details	binding site for residue PKP G 501

Chain	Residue
G	GLY98
G	ALA99
G	PHE115
G	GLY137
G	GLY138
G	TYR141
H	ALA300
H	TYR326
H	GLY341
H	LEU345
H	GLY366
H	ALA370
H	VAL391

site_id	AC8
Number of Residues	12
Details	binding site for residue PKP H 501

Chain	Residue
G	GLY341
G	LEU345
G	GLY366
G	ALA370
H	GLY98
H	ALA99
H	PHE115
H	GLY137
H	GLY138
H	TYR141
G	ALA300
G	TYR326

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	BINDING: BINDING => ECO:0007744\|PDB:4G2R

Chain	Residue	Details
A	ALA99
C	GLY138
C	HIS185
C	TRP334
D	ALA99
D	GLY138
D	HIS185
D	TRP334
E	ALA99
E	GLY138
E	HIS185
A	GLY138
E	TRP334
F	ALA99
F	GLY138
F	HIS185
F	TRP334
G	ALA99
G	GLY138
G	HIS185
G	TRP334
H	ALA99
A	HIS185
H	GLY138
H	HIS185
H	TRP334
A	TRP334
B	ALA99
B	GLY138
B	HIS185
B	TRP334
C	ALA99

site_id	SWS_FT_FI2
Number of Residues	8
Details	MOD_RES: N-acetylthreonine => ECO:0007744\|PubMed:21969609

Chain	Residue	Details
A	THR2
B	THR2
C	THR2
D	THR2
E	THR2
F	THR2
G	THR2
H	THR2

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