Structure of PDB 4mv7 Chain A

Receptor sequence
>4mv7A (length=414) Species: 71421 (Haemophilus influenzae Rd KW20) [Search protein sequence]
MLEKVVIANRGEIALRILRACKELGIKTVAVHSTADRDLKHVLLADETIC
IGPAPSAKSYLNIPAIIAAAEVTGADAIHPGYGFLSENADFAEQVERSGF
TFIGPTADVIRLMGDKVSAIKAMKKAGVPCVPGSAKNKEIAKRIGYPIII
RVVRSEDALEESIAMTKAEMEKYLENPRHVEIQVLADTHGNAVYLAERDC
SMQRRHQKVVEEAPAPGITEEVRRDIGSRCANACVEIGYRGAGTFEFLYE
NGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQLRIAAGLPISFKQEDIKV
KGHAMECRINAEDPKTFLPSPGKVNHLHSPGGLGVRWDSHVYGGYTVPPH
YDSMIAKLITYGDTREVAIRRMQNALSETIIDGIKTNIPLHELILEDENF
QKGGTNIHYLEKKL
3D structure
PDB4mv7 Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase.
ChainA
Resolution1.73 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 H209 R235 T274 E276 E288 N290 R292 E296 R338
Catalytic site (residue number reindexed from 1) K116 H179 R205 T244 E246 E258 N260 R262 E266 R308
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 PPF A K238 R292 Q294 V295 E296 R338 K208 R262 Q264 V265 E266 R308
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:4mv7, PDBe:4mv7, PDBj:4mv7
PDBsum4mv7
PubMed26020841
UniProtP43873|ACCC_HAEIN Biotin carboxylase (Gene Name=accC)

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