2W71

Crystal structure of Biotin carboxylase from E. coli in complex with the imidazole-pyrimidine inhibitor

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	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
C	0000166	molecular_function	nucleotide binding
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	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006633	biological_process	fatty acid biosynthetic process
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 1447

Chain	Residue
A	ARG292
A	GLN294
A	VAL295
A	HOH2149

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C 1447

Chain	Residue
C	ARG292
C	GLN294
C	VAL295
C	HOH2185

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE L23 A 1448

Chain	Residue
A	LYS159
A	GLY165
A	GLU201
A	LYS202
A	TYR203
A	LEU204
A	HIS209
A	GLN233
A	HIS236
A	LEU278
A	ILE287
A	GLU288
A	ILE437
A	ILE157

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE L23 C 1448

Chain	Residue
C	ILE157
C	LYS159
C	GLY165
C	MET169
C	GLU201
C	LYS202
C	TYR203
C	LEU204
C	HIS209
C	GLN233
C	HIS236
C	LEU278
C	ILE287
C	GLU288
C	ILE437

---

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	888
Details	Domain: {"description":"Biotin carboxylation"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
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_FI3
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
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_FI5
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_FI6
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_FI7
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_FI8
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

---

site_id	SWS_FT_FI9
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---