Structure of PDB 2iby Chain D

Receptor sequence
>2ibyD (length=393) Species: 9606 (Homo sapiens) [Search protein sequence]
SKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKE
EVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIM
MASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGL
TDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNE
VIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANAS
TLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAAS
MVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLG
HPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
3D structure
PDB2iby Crystallographic and Kinetic Studies of Human Mitochondrial Acetoacetyl-CoA Thiolase: The Importance of Potassium and Chloride Ions for Its Structure and Function
ChainD
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) C126 H385 C413 G415
Catalytic site (residue number reindexed from 1) C92 H351 C379 G381
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 K D Y219 A280 A281 A283 S284 V381 Y185 A246 A247 A249 S250 V347
BS02 COA D C126 L184 H192 M193 Y219 V259 D260 K263 L267 F271 S284 F356 C92 L150 H158 M159 Y185 V225 D226 K229 L233 F237 S250 F322
Gene Ontology
Molecular Function
GO:0003985 acetyl-CoA C-acetyltransferase activity
GO:0003988 acetyl-CoA C-acyltransferase activity
GO:0016453 C-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0019899 enzyme binding
GO:0030955 potassium ion binding
GO:0034736 cholesterol O-acyltransferase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0120225 coenzyme A binding
Biological Process
GO:0001889 liver development
GO:0006085 acetyl-CoA biosynthetic process
GO:0006550 isoleucine catabolic process
GO:0006631 fatty acid metabolic process
GO:0006635 fatty acid beta-oxidation
GO:0009725 response to hormone
GO:0014070 response to organic cyclic compound
GO:0015936 coenzyme A metabolic process
GO:0015937 coenzyme A biosynthetic process
GO:0042594 response to starvation
GO:0046356 acetyl-CoA catabolic process
GO:0046952 ketone body catabolic process
GO:0060612 adipose tissue development
GO:0072229 metanephric proximal convoluted tubule development
GO:1902224 ketone body metabolic process
GO:1902860 propionyl-CoA biosynthetic process
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0005783 endoplasmic reticulum
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2iby, PDBe:2iby, PDBj:2iby
PDBsum2iby
PubMed17371050
UniProtP24752|THIL_HUMAN Acetyl-CoA acetyltransferase, mitochondrial (Gene Name=ACAT1)

[Back to BioLiP]