4MV4

Crystal Structure of Biotin Carboxylase from Haemophilus influenzae in Complex with AMPPCP and Mg2

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	0005524	molecular_function	ATP binding
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	0046872	molecular_function	metal ion binding
A	2001295	biological_process	malonyl-CoA biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ACP A 501

Chain	Residue
A	LYS159
A	GLU288
A	MG505
A	HOH708
A	HOH901
A	GLY164
A	MET169
A	GLU201
A	LYS202
A	TYR203
A	LEU204
A	HIS236
A	LEU278

---

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 502

Chain	Residue
A	LEU2

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 503

Chain	Residue
A	SER359
A	PRO360
A	GLY361

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 504

Chain	Residue
A	ARG292
A	GLN294
A	VAL295
A	HOH745
A	HOH895

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 505

Chain	Residue
A	GLU276
A	GLU288
A	ASN290
A	ACP501
A	HOH901

---

Functional Information from PROSITE/UniProt

site_id	PS00866
Number of Residues	15
Details	CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPIIIKASgggGGrG

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	1
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P24182

Chain	Residue	Details
A	ARG292

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:26020841, ECO:0007744|PDB:4MV8

Chain	Residue	Details
A	LYS116

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:26020841, ECO:0007744|PDB:4MV3, ECO:0007744|PDB:4MV4

Chain	Residue	Details
A	LYS159

---

site_id	SWS_FT_FI4
Number of Residues	7
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P24182

Chain	Residue	Details
A	GLY165
A	HIS209
A	HIS236
A	LYS238
A	ARG292
A	VAL295
A	ARG338

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:26020841, ECO:0007744|PDB:4MV1, ECO:0007744|PDB:4MV3, ECO:0007744|PDB:4MV4, ECO:0007744|PDB:4MV8, ECO:0007744|PDB:4RZQ

Chain	Residue	Details
A	GLU201

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409

Chain	Residue	Details
A	GLU276
A	GLU288
A	ASN290

---