1BNC	Fatty Acid Biosynthesis	date	Jul 06, 1994
authors	G.Waldrop, I.Rayment, H.M.Holden
compound		source
Molecule: Biotin Carboxylase Chain: A, B Ec: 6.3.4.14		Organism_scientific: Escherichia Coli
symmetry	Space Group: P 21 21 21	R_factor
crystal cell	length a length b length c angle alpha angle beta angle gamma 61.900 96.100 180.600 90.00 90.00 90.00
method	X-Ray Diffraction	resolution	2.4 Å
ligand	PO4	enzyme	Biotin carboxylase;. Biotin carboxylase (component of acetyl CoA carboxylase). Ligase E.C.6.3.4.14 BRENDA
similarity	Contains 1 biotin carboxylation domain. Contains 1 atp-grasp domain.[Biotin_carb_C]
subunit	Acetyl-coa carboxylase is an heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2. 2 complex.
catalytic activ.	Atp + biotin-carboxyl-carrier protein + co(2) = adp + phosphate + carboxybiotin-carboxyl-carrier protein.
pathway	Long-chain fatty acid biosynthesis; first step.
gene	accC (E. coli)
function	This protein is a component of the acetyl coenzyme a carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-coa.
Gene Ontology	Chain Function Process Component A, B nucleotide binding catalytic activity acetyl-CoA carboxylase activ... biotin carboxylase activity ATP binding biotin binding ligase activity fatty acid biosynthetic proc... metabolic process lipid biosynthetic process
Primary reference	Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase., Waldrop GL, Rayment I, Holden HM, Biochemistry 1994 Aug 30;33(34):10249-56. PMID:7915138

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (166 Kb) [Save to disk] Biological Unit Coordinates (1bnc.pdb1.gz) 137 Kb CSU: Contacts of Structural Units for 1BNC Likely Quarternary Molecular Structure file(s) for 1BNC Retrieve 1BNC in mmCIF format [Save to disk]

View 1BNC in 3D

On Jmol, a nice Rasmol like molecule viewer. This is good for easiest viewing of basic structure. On FirstGlance, an excellent tool for a guided tour on the structure components, by E. Martz. On AstexViewer, from MSD-EBI (viewer documentation). On RasMol (Install RasMol freeware) Here's help on how to use RasMol.

Visual 3D analysis of 1BNC

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Structure-derived information

Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1BNC, from MSDmotif at EBI Genome occurence of 1BNC's fold from GeneCensus Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1bnca2, region A:1-114 [Jmol] [rasmolscript] [script source]     - Domain d1bnca3, region A:115-330 [Jmol] [rasmolscript] [script source]     - Domain d1bnca1, region A:331-446 [Jmol] [rasmolscript] [script source]     - Domain d1bncb2, region B:1-114 [Jmol] [rasmolscript] [script source]     - Domain d1bncb3, region B:115-330 [Jmol] [rasmolscript] [script source]     - Domain d1bncb1, region B:331-448 [Jmol] [rasmolscript] [script source] Fold representative 1bnc from FSSP and Dali (Families of Structurally Similar Proteins) Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH Summaries and structural analyses of PDB data files from PDBSum Identification of Protein Pockets & Cavities at CASTp

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1bnc_A] [1bnc_B]

Other resources with information on 1BNC

InterPro: IPR011764 , IPR011761 , IPR005482 , IPR005481 , IPR005479 , IPR004549 PDBREPORT (protein verification by WHAT_CHECK procedures) MMDB (Entrez's Structure Database)

Movements, Movies and Images

Domain movements in 1BNC from the Database of Macromolecular Movements. Images from IMB Jena Image Library of Biological Macromolecules.

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