Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3RV3

Crystal structure of E.coli biotin carboxylase in complex with two ADP and one Mg ion

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
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	0000166	molecular_function	nucleotide binding
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	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ADP A 1000

Chain	Residue
A	TYR82
A	LYS238
A	ASN290
A	ARG292
A	GLN294
A	VAL295
A	GLU296
A	ARG338
A	ASP382
A	HOH547
A	HOH561
A	GLY83
A	HOH699
A	HOH747
A	HOH758
A	GLY162
A	GLY163
A	GLY164
A	GLY165
A	ARG167
A	PHE193
A	GLN237

site_id	AC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP A 1002

Chain	Residue
A	LYS116
A	LYS159
A	GLY163
A	GLY164
A	GLY165
A	GLY166
A	MET169
A	GLU201
A	LYS202
A	TYR203
A	LEU204
A	HIS209
A	GLN233
A	HIS236
A	GLU276
A	LEU278
A	ILE287
A	GLU288
A	ILE437
A	HOH547
A	HOH668
A	HOH684
A	HOH736
A	HOH758
A	HOH804
A	MG1004

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1004

Chain	Residue
A	GLU276
A	GLU288
A	HOH547
A	HOH684
A	HOH804
A	ADP1002

site_id	AC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ADP B 1001

Chain	Residue
B	LYS116
B	LYS159
B	GLY164
B	GLY165
B	GLY166
B	MET169
B	GLU201
B	LYS202
B	TYR203
B	LEU204
B	HIS209
B	GLN233
B	HIS236
B	GLU276
B	LEU278
B	ILE287
B	GLU288
B	ILE437
B	HOH545
B	HOH561
B	HOH582
B	HOH732
B	MG1005

site_id	AC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ADP B 1003

Chain	Residue
B	HOH807
B	HOH821
B	TYR82
B	GLY83
B	GLY162
B	GLY163
B	GLY164
B	GLY165
B	PHE193
B	LYS238
B	ASN290
B	ARG292
B	GLN294
B	VAL295
B	GLU296
B	ARG338
B	ASP382
B	HOH510
B	HOH523
B	HOH543
B	HOH641
B	HOH651
B	HOH732
B	HOH771

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 1005

Chain	Residue
B	GLU276
B	GLU288
B	HOH545
B	HOH732
B	ADP1001

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	394
Details	Domain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10821865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8D","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8D","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10821865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8D","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10821865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details