Structure of PDB 4mv3 Chain A

Receptor sequence
>4mv3A (length=439) Species: 71421 (Haemophilus influenzae Rd KW20) [Search protein sequence]
MLEKVVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETIC
IGPAPSAKSYLNIPAIIAAAEVTGADAIHPGYGFLSENADFAEQVERSGF
TFIGPTADVIRLMGDKVSAIKAMKKAGVPCVPGSDGPVSNDIAKNKEIAK
RIGYPIIIKASGMRVVRSEDALEESIAMTKAEAKAAFNNDMVYMEKYLEN
PRHVEIQVLADTHGNAVYLAERDCSMQRRHQKVVEEAPAPGITEEVRRDI
GSRCANACVEIGYRGAGTFEFLYENGEFYFIEMNTRIQVEHPVTEMITGV
DLVKEQLRIAAGLPISFKQEDIKVKGHAMECRINAEDPKTFLPSPGKVNH
LHSPGGLGVRWDSHVYGGYTVPPHYDSMIAKLITYGDTREVAIRRMQNAL
SETIIDGIKTNIPLHELILEDENFQKGGTNIHYLEKKLG
3D structure
PDB4mv3 Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase.
ChainA
Resolution1.69 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) K116 K159 D190 H203 R229 T268 E270 E282 N284 R286 E290 R332
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 ACP A K159 M169 E201 Y203 L204 E276 L278 E288 K159 M163 E195 Y197 L198 E270 L272 E282
BS02 BCT A R292 Q294 V295 R286 Q288 V289
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4mv3, PDBe:4mv3, PDBj:4mv3
PDBsum4mv3
PubMed26020841
UniProtP43873|ACCC_HAEIN Biotin carboxylase (Gene Name=accC)

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