3JZF

Crystal structure of biotin carboxylase from E. Coli in complex with benzimidazoles series

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	6
Details	BINDING SITE FOR RESIDUE CO3 A 466

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

---

site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE JZK B 466

Chain	Residue
B	GLY164
B	GLY165
B	GLY166
B	ARG167
B	GLY168
B	MET169
B	TYR199
B	GLU201
B	LYS202
B	TYR203
B	LEU204
B	HIS209
B	HIS236
B	LEU278
B	ILE287
B	GLU288
B	LYS116
B	LYS159
B	ALA160

---

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	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
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_FI3
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_FI4
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_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	444
Details	Domain: {"description":"Biotin carboxylation"}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	197
Details	Domain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
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_FI9
Number of Residues	3
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

---