6P7U

CRYSTAL STRUCTURE OF THE CARBOXYLTRANSFERASE SUBUNIT OF ACC (ACCD6) IN COMPLEX WITH INHIBITOR QUIZALOFOP-P 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue FTJ A 501

Chain	Residue
A	GLY98
B	GLY341
B	LEU345
B	GLY366
B	ILE369
B	ALA370
A	ALA99
A	PHE115
A	GLY137
A	GLY138
A	TYR141
B	LEU295
B	ALA300
B	TYR326

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site_id	AC2
Number of Residues	16
Details	binding site for residue FTJ B 501

Chain	Residue
A	LEU295
A	ALA300
A	TYR326
A	GLY341
A	LEU345
A	GLY366
A	ILE369
A	ALA370
A	VAL391
B	GLY98
B	ALA99
B	PHE115
B	GLY137
B	GLY138
B	TYR141
B	HOH603

---

site_id	AC3
Number of Residues	13
Details	binding site for residue FTJ 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	ILE369
D	ALA370

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site_id	AC4
Number of Residues	13
Details	binding site for residue FTJ D 501

Chain	Residue
C	ALA300
C	TYR326
C	GLY341
C	LEU345
C	GLY366
C	ILE369
C	ALA370
D	GLY98
D	ALA99
D	PHE115
D	GLY137
D	GLY138
D	TYR141

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0007744|PDB:4G2R

Chain	Residue	Details
D	ALA99
D	GLY138
D	HIS185
D	TRP334
A	TRP334
B	ALA99
B	GLY138
B	HIS185
B	TRP334
C	ALA99
C	GLY138
C	HIS185
C	TRP334
A	ALA99
A	GLY138
A	HIS185

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site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609

Chain	Residue	Details
B	THR2
C	THR2
D	THR2
A	THR2

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