Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2GPW

Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003989	molecular_function	acetyl-CoA carboxylase activity
A	0004075	molecular_function	biotin carboxylase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006633	biological_process	fatty acid biosynthetic process
A	0009317	cellular_component	acetyl-CoA carboxylase complex
A	0016874	molecular_function	ligase activity
A	0042803	molecular_function	protein homodimerization activity
A	0045717	biological_process	negative regulation of fatty acid biosynthetic process
A	0046872	molecular_function	metal ion binding
A	2001295	biological_process	malonyl-CoA biosynthetic process
B	0003824	molecular_function	catalytic activity
B	0003989	molecular_function	acetyl-CoA carboxylase activity
B	0004075	molecular_function	biotin carboxylase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006633	biological_process	fatty acid biosynthetic process
B	0009317	cellular_component	acetyl-CoA carboxylase complex
B	0016874	molecular_function	ligase activity
B	0042803	molecular_function	protein homodimerization activity
B	0045717	biological_process	negative regulation of fatty acid biosynthetic process
B	0046872	molecular_function	metal ion binding
B	2001295	biological_process	malonyl-CoA biosynthetic process
C	0003824	molecular_function	catalytic activity
C	0003989	molecular_function	acetyl-CoA carboxylase activity
C	0004075	molecular_function	biotin carboxylase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006633	biological_process	fatty acid biosynthetic process
C	0009317	cellular_component	acetyl-CoA carboxylase complex
C	0016874	molecular_function	ligase activity
C	0042803	molecular_function	protein homodimerization activity
C	0045717	biological_process	negative regulation of fatty acid biosynthetic process
C	0046872	molecular_function	metal ion binding
C	2001295	biological_process	malonyl-CoA biosynthetic process
D	0003824	molecular_function	catalytic activity
D	0003989	molecular_function	acetyl-CoA carboxylase activity
D	0004075	molecular_function	biotin carboxylase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006633	biological_process	fatty acid biosynthetic process
D	0009317	cellular_component	acetyl-CoA carboxylase complex
D	0016874	molecular_function	ligase activity
D	0042803	molecular_function	protein homodimerization activity
D	0045717	biological_process	negative regulation of fatty acid biosynthetic process
D	0046872	molecular_function	metal ion binding
D	2001295	biological_process	malonyl-CoA biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00866
Number of Residues	15
Details	CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVIIKASgggGGrG

Chain	Residue	Details
A	TYR154-GLY168

site_id	PS00867
Number of Residues	8
Details	CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FIEMNTRI

Chain	Residue	Details
A	PHE286-ILE293

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000269\|PubMed:19213731

Chain	Residue	Details
A	ARG292
B	ARG292
C	ARG292
D	ARG292

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:10821865, ECO:0000269\|PubMed:19213731, ECO:0007744\|PDB:1DV2, ECO:0007744\|PDB:3G8D

Chain	Residue	Details
A	LYS116
A	GLY165
B	LYS116
B	GLY165
C	LYS116
C	GLY165
D	LYS116
D	GLY165

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:19213731, ECO:0007744\|PDB:3G8C, ECO:0007744\|PDB:3G8D

Chain	Residue	Details
A	LYS159
B	LYS159
C	LYS159
D	LYS159

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:10821865, ECO:0000269\|PubMed:19213731, ECO:0007744\|PDB:1DV2, ECO:0007744\|PDB:3G8C, ECO:0007744\|PDB:3G8D

Chain	Residue	Details
A	GLU201
B	GLU201
C	GLU201
D	GLU201

site_id	SWS_FT_FI5
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:19213731, ECO:0007744\|PDB:3G8C

Chain	Residue	Details
A	HIS209
B	ARG338
C	HIS209
C	LYS238
C	ARG292
C	VAL295
C	ARG338
D	HIS209
D	LYS238
D	ARG292
D	VAL295
A	LYS238
D	ARG338
A	ARG292
A	VAL295
A	ARG338
B	HIS209
B	LYS238
B	ARG292
B	VAL295

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:10821865, ECO:0000269\|PubMed:19213731, ECO:0007744\|PDB:1DV2, ECO:0007744\|PDB:3G8C

Chain	Residue	Details
A	HIS236
B	HIS236
C	HIS236
D	HIS236

site_id	SWS_FT_FI7
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00409

Chain	Residue	Details
A	GLU276
D	GLU276
D	GLU288
D	ASN290
A	GLU288
A	ASN290
B	GLU276
B	GLU288
B	ASN290
C	GLU276
C	GLU288
C	ASN290

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