3G8C

Crystal Structure of Biotin Carboxylase in Complex with Biotin, Bicarbonate, ADP and Mg Ion

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	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	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 A1000

Chain	Residue
A	LYS116
A	TYR203
A	LEU204
A	HIS209
A	GLN233
A	HIS236
A	GLU276
A	LEU278
A	GLU288
A	ILE437
A	HOH538
A	ILE157
A	HOH592
A	HOH796
A	MG1002
A	LYS159
A	GLY163
A	GLY164
A	GLY165
A	MET169
A	GLU201
A	LYS202

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A1002

Chain	Residue
A	GLU276
A	GLU288
A	HOH538
A	HOH640
A	ADP1000

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE BTN A1004

Chain	Residue
A	TYR82
A	PHE84
A	ARG292
A	VAL295
A	ARG338
A	TYR381
A	ASP382
A	HOH483
A	HOH486
A	HOH550
A	HOH613
A	HOH755
A	BCT1006

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT A1006

Chain	Residue
A	LYS238
A	ASN290
A	ARG292
A	GLN294
A	VAL295
A	GLU296
A	ARG338
A	HOH756
A	BTN1004

---

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP B1001

Chain	Residue
B	LYS116
B	ILE157
B	LYS159
B	GLY165
B	GLY166
B	MET169
B	GLU201
B	LYS202
B	TYR203
B	LEU204
B	HIS209
B	GLN233
B	GLU276
B	LEU278
B	ILE287
B	GLU288
B	ILE437
B	HOH503
B	HOH575
B	HOH810
B	MG1003

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B1003

Chain	Residue
B	GLU276
B	GLU288
B	HOH753
B	HOH804
B	ADP1001

---

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BTN B1005

Chain	Residue
B	TYR82
B	PHE84
B	GLN237
B	ARG292
B	VAL295
B	ARG338
B	TYR381
B	ASP382
B	HOH490
B	HOH521
B	HOH716
B	HOH762
B	HOH851
B	HOH872
B	BCT1007

---

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT B1007

Chain	Residue
B	LYS238
B	ASN290
B	ARG292
B	GLN294
B	VAL295
B	GLU296
B	ARG338
B	HOH841
B	BTN1005

---

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
B	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
B	LYS116
B	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
B	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
B	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
B	ARG338
A	LYS238
A	ARG292
A	VAL295
A	ARG338
B	HIS209
B	LYS238
B	ARG292
B	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
B	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
B	GLU276
B	GLU288
B	ASN290

---