Structure of PDB 3ouz Chain A

Receptor sequence
>3ouzA (length=445) Species: 192222 (Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819) [Search protein sequence]
NAMEIKSILIANRGEIALRALRTIKEMGKKAICVYSEADKDALYLKYADA
SICIGKARSSESYLNIPAIIAAAEIAEADAIFPGYGFLSENQNFVEICAK
HNIKFIGPSVEAMNLMSDKSKAKQVMQRAGVPVIPGSDGALAGAEAAKKL
AKEIGYPVILKAAAGGGGRGMRVVENEKDLEKAYWSAESEAMTAFGDGTM
YMEKYIQNPRHIEVQVIGDSFGNVIHVGERDCSMQRRHQKLIEESPAILL
DEKTRTRLHETAIKAAKAIGYEGAGTFEFLVDKNLDFYFIEMNTRLQVEH
CVSEMVSGIDIIEQMIKVAEGYALPSQESIKLNGHSIECRITAEDSKTFL
PSPGKITKYIPPAGRNVRMESHCYQDYSVPAYYDSMIGKLVVWAEDRNKA
IAKMKVALDELLISGIKTTKDFHLSMMENPDFINNNYDTNYLARH
3D structure
PDB3ouz Crystal Structure of Biotin Carboxylase-ADP complex from Campylobacter jejuni
ChainA
Resolution1.902 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K159 G165 G166 H209 K238 T274 E276 E289 N291 V296 E297 R338
Catalytic site (residue number reindexed from 1) K161 G167 G168 H211 K240 T276 E278 E291 N293 V298 E299 R340
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 ADP A K117 I157 K159 G164 G166 M169 E201 Y203 I204 H209 Q233 L278 E289 T437 K119 I159 K161 G166 G168 M171 E203 Y205 I206 H211 Q235 L280 E291 T439
BS02 MG A E276 E289 E278 E291
Gene Ontology
Molecular Function
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3ouz, PDBe:3ouz, PDBj:3ouz
PDBsum3ouz
PubMed
UniProtQ0P8W7

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