2W6O

Crystal structure of Biotin carboxylase from E. coli in complex with 4-Amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment

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
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OA3 A 1446

Chain	Residue
A	ILE157
A	LYS159
A	LYS202
A	TYR203
A	LEU204
A	LEU278
A	ILE437
A	HOH2032

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OA3 C 1447

Chain	Residue
C	MET169
C	LYS202
C	TYR203
C	LEU204
C	LEU278
C	LYS159

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 1447

Chain	Residue
A	ARG292
A	VAL295

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 1448

Chain	Residue
C	ARG292
C	GLN294
C	VAL295

---

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	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:19213731

Chain	Residue	Details
A	ARG292
C	ARG292

---

site_id	SWS_FT_FI2
Number of Residues	4
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

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D

Chain	Residue	Details
A	LYS159
C	LYS159

---

site_id	SWS_FT_FI4
Number of Residues	2
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

---

site_id	SWS_FT_FI5
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C

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

---

site_id	SWS_FT_FI6
Number of Residues	2
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

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409

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

---