Structure of PDB 2vqd Chain A

Receptor sequence

>2vqdA (length=447) Species: 287 (Pseudomonas aeruginosa)

MLEKVLIANRGEIALRILRACKELGIKTVAVHSTADRELMHLSLADESVC
IGPAPATQSYLQIPAIIAAAEVTGATAIHPGYGFLAENADFAEQIERSGF
TFVGPTAEVIRLMGDKVSAKDAMKRAGVPTVPGSDGPLPEDEETALAIAR
EVGYPVIIKAAGGGGGRGMRVVYDESELIKSAKLTRTEAGAAFGNPMVYL
EKFLTNPRHVEVQVLSDGQGNAIHLGDRDCSLQRRHQKVIEEAPAPGIDE
KARQEVFARCVQACIEIGYRGAGTFEFLYENGRFYFIEMNTRVQVEHPVS
EMVTGVDIVKEMLRIASGEKLSIRQEDVVIRGHALECRINAEDPKTFMPS
PGKVKHFHAPGGNGVRVDSHLYSGYSVPPNYDSLVGKVITYGADRDEALA
RMRNALDELIVDGIKTNTELHKDLVRDAAFCKGGVNIHYLEKKLGMD

3D structure

• PDB: 2vqd Structural Evidence for Substrate-Induced Synergism and Half-Sites Reactivity in Biotin Carboxylase.
• Chain: A
• Resolution: 2.41 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K116 K159 P196 H209 R235 T274 E276 E288 N290 R292 E296 R338
• Catalytic site (residue number reindexed from 1): K116 K159 P196 H209 R235 T274 E276 E288 N290 R292 E296 R338
• Enzyme Commision number: 6.3.4.14: biotin carboxylase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	AP2	A	K116 I157 K159 G164 G166 F203 L204 H209 Q233 H236 L278 E288 I437	K116 I157 K159 G164 G166 F203 L204 H209 Q233 H236 L278 E288 I437
BS02	MG	A	E276 E288	E276 E288

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0003989 acetyl-CoA carboxylase activity
• GO:0004075 biotin carboxylase activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006633 fatty acid biosynthetic process
• GO:2001295 malonyl-CoA biosynthetic process

External links

• PDB: RCSB:2vqd, PDBe:2vqd, PDBj:2vqd
• PDBsum: 2vqd
• PubMed: 18725455
• UniProt: P37798|ACCC_PSEAE Biotin carboxylase (Gene Name=accC)