Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4HR7

Crystal Structure of Biotin Carboxyl Carrier Protein-Biotin Carboxylase Complex from E.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	0003989	molecular_function	acetyl-CoA carboxylase activity
B	0005515	molecular_function	protein 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	0060090	molecular_function	molecular adaptor activity
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	0003989	molecular_function	acetyl-CoA carboxylase activity
D	0005515	molecular_function	protein 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	0060090	molecular_function	molecular adaptor activity
D	2001295	biological_process	malonyl-CoA biosynthetic process
E	0003824	molecular_function	catalytic activity
E	0003989	molecular_function	acetyl-CoA carboxylase activity
E	0004075	molecular_function	biotin carboxylase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006633	biological_process	fatty acid biosynthetic process
E	0009317	cellular_component	acetyl-CoA carboxylase complex
E	0016874	molecular_function	ligase activity
E	0042803	molecular_function	protein homodimerization activity
E	0045717	biological_process	negative regulation of fatty acid biosynthetic process
E	0046872	molecular_function	metal ion binding
E	2001295	biological_process	malonyl-CoA biosynthetic process
F	0003824	molecular_function	catalytic activity
F	0003989	molecular_function	acetyl-CoA carboxylase activity
F	0004075	molecular_function	biotin carboxylase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006633	biological_process	fatty acid biosynthetic process
F	0009317	cellular_component	acetyl-CoA carboxylase complex
F	0016874	molecular_function	ligase activity
F	0042803	molecular_function	protein homodimerization activity
F	0045717	biological_process	negative regulation of fatty acid biosynthetic process
F	0046872	molecular_function	metal ion binding
F	2001295	biological_process	malonyl-CoA biosynthetic process
G	0003989	molecular_function	acetyl-CoA carboxylase activity
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006633	biological_process	fatty acid biosynthetic process
G	0009317	cellular_component	acetyl-CoA carboxylase complex
G	0060090	molecular_function	molecular adaptor activity
G	2001295	biological_process	malonyl-CoA biosynthetic process
I	0003989	molecular_function	acetyl-CoA carboxylase activity
I	0005515	molecular_function	protein binding
I	0005737	cellular_component	cytoplasm
I	0005829	cellular_component	cytosol
I	0006633	biological_process	fatty acid biosynthetic process
I	0009317	cellular_component	acetyl-CoA carboxylase complex
I	0060090	molecular_function	molecular adaptor activity
I	2001295	biological_process	malonyl-CoA biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 501

Chain	Residue
A	SER56
A	TYR380
A	TYR381
A	HOH660
B	ARG84

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 502

Chain	Residue
A	GLU296
A	ARG338
A	HOH636
A	LYS238
A	ARG292
A	GLN294
A	VAL295

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 503

Chain	Residue
A	PRO250
A	ARG253
A	VAL330
A	HOH666

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 504

Chain	Residue
A	SER34
A	ALA35
A	HOH669
A	HOH672
A	HOH704
E	SER34
E	ALA35
E	ALA54

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 505

Chain	Residue
A	ARG10
A	HIS370
A	TYR375
A	VAL377
A	PRO378
A	ILE385

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 501

Chain	Residue
C	SER56
C	TYR380
C	TYR381
C	HOH647
D	ILE82
D	ARG84

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 502

Chain	Residue
C	LYS238
C	ARG292
C	GLN294
C	VAL295
C	GLU296
C	ARG338

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 503

Chain	Residue
C	ASP229
C	CYS230
C	SER231
C	MET232
C	VAL240
C	GLU242
C	THR435

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 501

Chain	Residue
E	SER56
E	TYR380
E	TYR381
I	ARG84

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 E 502

Chain	Residue
E	LYS238
E	ARG292
E	GLN294
E	VAL295
E	GLU296
E	ARG338
E	HOH714

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 503

Chain	Residue
E	ARG10
E	HIS370
E	TYR375
E	VAL377
E	PRO378
E	ILE385

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 501

Chain	Residue
F	PRO55
F	SER56
F	TYR381
F	HOH671
G	ILE82
G	ARG84

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 502

Chain	Residue
F	LYS238
F	ARG292
F	GLN294
F	VAL295
F	GLU296
F	ARG338

Functional Information from PROSITE/UniProt

site_id	PS00188
Number of Residues	18
Details	BIOTIN Biotin-requiring enzymes attachment site. GDtLciVeAMKMmnqIeA

Chain	Residue	Details
B	GLY112-ALA129

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	MOD_RES: N6-biotinyllysine => ECO:0000255\|PROSITE-ProRule:PRU01066, ECO:0000269\|PubMed:324999

Chain	Residue	Details
B	LYS122
D	LYS122
G	LYS122
I	LYS122

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
C	LYS116
C	GLY165
E	LYS116
E	GLY165
F	LYS116
F	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
C	LYS159
E	LYS159
F	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
C	GLU201
E	GLU201
F	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
C	ARG338
E	HIS209
E	LYS238
E	ARG292
E	VAL295
E	ARG338
F	HIS209
F	LYS238
F	ARG292
F	VAL295
A	LYS238
F	ARG338
A	ARG292
A	VAL295
A	ARG338
C	HIS209
C	LYS238
C	ARG292
C	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
C	HIS236
E	HIS236
F	HIS236

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

Chain	Residue	Details
A	GLU276
F	GLU276
F	GLU288
F	ASN290
A	GLU288
A	ASN290
C	GLU276
C	GLU288
C	ASN290
E	GLU276
E	GLU288
E	ASN290

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