Structure of PDB 4mv8 Chain A

Receptor sequence
>4mv8A (length=431) Species: 71421 (Haemophilus influenzae Rd KW20) [Search protein sequence]
MLEKVVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETIC
IGPAPSAKSYLNIPAIIAAAEVTGADAIHPGYGFLSENADFAEQVERSGF
TFIGPTADVIRLMGDKVSAIKAMKKAGVPCVPGSDGPVSNDIAKNKEIAK
RIGYPIIIKASGGMRVVRSEDALEESIAMTDMVYMEKYLENPRHVEIQVL
ADTHGNAVYLAERDCSMQRRHQKVVEEAPAPGITEEVRRDIGSRCANACV
EIGYRGAGTFEFLYENGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQLRI
AAGLPISFKQEDIKVKGHAMECRINAEDPKTFLPSPGKVNHLHSPGGLGV
RWDSHVYGGYTVPPHYDSMIAKLITYGDTREVAIRRMQNALSETIIDGIK
TNIPLHELILEDENFQKGGTNIHYLEKKLGM
3D structure
PDB4mv8 Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase.
ChainA
Resolution2.06 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 D181 H194 R220 T259 E261 E273 N275 R277 E281 R323
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 PO4 A K238 R292 Q294 V295 E296 R338 K223 R277 Q279 V280 E281 R323
BS02 ACP A K116 K159 M169 L204 H236 L278 K116 K159 M164 L189 H221 L263
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:4mv8, PDBe:4mv8, PDBj:4mv8
PDBsum4mv8
PubMed26020841
UniProtP43873|ACCC_HAEIN Biotin carboxylase (Gene Name=accC)

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