4MV1

Crystal Structure of Biotin Carboxylase from Haemophilus influenzae in Complex with ADP and Phosphate

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	9
Details	BINDING SITE FOR RESIDUE PO4 A 501

Chain	Residue
A	LYS238
A	ARG292
A	GLN294
A	VAL295
A	GLU296
A	ARG338
A	HOH772
A	HOH773
A	HOH789

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE ADP A 502

Chain	Residue
A	LYS116
A	LYS159
A	GLU201
A	LYS202
A	TYR203
A	LEU204
A	HIS236
A	LEU278
A	ILE437

---

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 503

Chain	Residue
A	LEU2

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 504

Chain	Residue
A	GLU175
A	ASP176
A	ASN436

---

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	Active site: {"evidences":[{"source":"UniProtKB","id":"P24182","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26020841","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MV8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26020841","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MV3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MV4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26020841","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MV1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MV3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MV4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MV8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RZQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P24182","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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