Structure of PDB 6bn2 Chain A

Receptor sequence
>6bn2A (length=393) Species: 1338011 (Elizabethkingia anophelis NUHP1) [Search protein sequence]
MKEVFIVSAVRTPMGSFMGSLSGVPATQLGAVAIKGALDKINLNPAEIQD
VYMGNVLQAGEGQAPAKQAALGAGLPNTTPTTAVNKVCASGMKAVMMAAQ
AVKAGDVEAIVAGGMENMSQVPHYIDGRNGVKLGDIKLQDGLLKDGLTDV
YSKQHMGNCAELCAKEYNITREEQDAFAIQSYERSAKAWSEGKFKEEVVP
VSIPQRKGEPIIFAEDEEYKNVKFDRIPTLPTVFQKENGTVTAANASTLN
DGASALVLMSKEKMESLGLKPLAKIVSYADAAQAPEWFTTAPAKALPIAL
AKANLTINDIDFFEFNEAFSVVGLANNKILGLDAAKVNVNGGAVALGHPL
GSSGSRIIVTLINVLKQNNAKYGAAAICNGGGGASAIVIENIK
3D structure
PDB6bn2 Crystal structure of Acetyl-CoA acetyltransferase from Elizabethkingia anophelis NUHP1
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C88 H348 C378 G380
Catalytic site (residue number reindexed from 1) C88 H348 C378 G380
Enzyme Commision number 2.3.1.9: acetyl-CoA C-acetyltransferase.
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 CA A Y182 A243 A244 A246 V344 Y182 A243 A244 A246 V344
Gene Ontology
Molecular Function
GO:0003985 acetyl-CoA C-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0046872 metal ion binding
Biological Process
GO:0006635 fatty acid beta-oxidation

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Molecular Function
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Biological Process
External links
PDB RCSB:6bn2, PDBe:6bn2, PDBj:6bn2
PDBsum6bn2
PubMed
UniProtA0A077EEP0

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