Structure of PDB 3rv3 Chain A

Receptor sequence
>3rv3A (length=447) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
GSHMLDKIVIANRGEIALRILRACKELGIKTVAVHSSADRDLKHVLLADE
TVCIGPAPSVKSYLNIPAIISAAEITGAVAIHPGYGFLSENANFAEQVER
SGFIFIGPKAETIRLMGDKVSAIAAMKKAGVPCVPGSDGPLGDDMDKNRA
IAKRIGYPVIIKASGGGGGRGMRVVRGDAELAQSISMTRAEAKAAFSNDM
VYMEKYLENPRHVEIQVLADGQGNAIYLAERDCSMQRRHQKVVEEAPAPG
ITPELRRYIGERCAKACVDIGYRGAGTFEFLFENGEFYFIEMNTRIQVEH
PVTEMITGVDLIKEQLRIAAGQPLSIKQEEVHVRGHAVECRINAEDPNTF
LPSPGKITRFHAPGGFGVRWESHIYAGYTVPPYYDSMIGKLICYGENRDV
AIARMKNALQELIIDGIKTNVDLQIRIMNDENFQHGGTNIHYLEKKL
3D structure
PDB3rv3 Structural and biochemical studies on the regulation of biotin carboxylase by substrate inhibition and dimerization.
ChainA
Resolution1.91 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K116 K159 D196 H209 R235 T274 E276 E288 N290 R292 E296 R338
Catalytic site (residue number reindexed from 1) K119 K162 D199 H212 R238 T277 E279 E291 N293 R295 E299 R341
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 Y82 G83 G164 G165 R167 F193 K238 R292 Q294 V295 E296 R338 D382 Y85 G86 G167 G168 R170 F196 K241 R295 Q297 V298 E299 R341 D385 PDBbind-CN: -logKd/Ki=2.00,IC50=10mM
BS02 ADP A K116 K159 G164 G165 G166 M169 E201 K202 Y203 L204 H209 Q233 H236 L278 E288 I437 K119 K162 G167 G168 G169 M172 E204 K205 Y206 L207 H212 Q236 H239 L281 E291 I440 PDBbind-CN: -logKd/Ki=2.00,IC50=10mM
BS03 MG A E276 E288 E279 E291
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003989 acetyl-CoA carboxylase activity
GO:0004075 biotin carboxylase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0045717 negative regulation of fatty acid biosynthetic process
GO:2001295 malonyl-CoA biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009317 acetyl-CoA carboxylase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3rv3, PDBe:3rv3, PDBj:3rv3
PDBsum3rv3
PubMed21592965
UniProtP24182|ACCC_ECOLI Biotin carboxylase (Gene Name=accC)

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