Structure of PDB 2ii4 Chain E

Receptor sequence
>2ii4E (length=234) Species: 9913 (Bos taurus) [Search protein sequence]
GKDRTEPVKGFHKAMVKTMSAALKIPHFGYCDEVDLTELVKLREELKPIA
FARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAM
DTEQGLIVPNVKNVQIRSIFEIATELNRLQKLGSAGQLSTNDLIGGTFTL
SNIGSIGGTYAKPVILPPEVAIGALGTIKALPRFNEKGEVCKAQIMNVSW
SADHRIIDGATVSRFSNLWKSYLENPAFMLLDLK
3D structure
PDB2ii4 A synchronized substrate-gating mechanism revealed by cubic-core structure of the bovine branched-chain alpha-ketoacid dehydrogenase complex.
ChainE
Resolution2.59 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) S338 H391
Catalytic site (residue number reindexed from 1) S151 H204
Enzyme Commision number 2.3.1.168: dihydrolipoyllysine-residue (2-methylpropanoyl)transferase.
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 COA E H391 G396 H204 G209
BS02 COA E R230 S245 M247 A286 M287 D288 L293 Q317 S338 N339 I340 G341 S342 T364 I365 R43 S58 M60 A99 M100 D101 L106 Q130 S151 N152 I153 G154 S155 T177 I178
Gene Ontology
Molecular Function
GO:0016746 acyltransferase activity

View graph for
Molecular Function
External links
PDB RCSB:2ii4, PDBe:2ii4, PDBj:2ii4
PDBsum2ii4
PubMed17124494
UniProtP11181|ODB2_BOVIN Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial (Gene Name=DBT)

[Back to BioLiP]