Structure of PDB 3uzb Chain B

Receptor sequence
>3uzbB (length=335) Species: 1299 (Deinococcus radiodurans) [Search protein sequence]
IDWSTLGFSYIRTDLRYLAHWKDGEWDAGTLTEDNQIHLAEGSTALHYGQ
QCFEGLKAYRCADGSINLFRPDQNAARMRMSCRRLLMPELSDEQFIDACL
QVVRANEHFLPPYGTGGSLYLRPFVIGVGDNIGVRTAPEFIFSVFCVPVG
PYFKGGLTPTNFITSDYDRAAPHGTGAAKVGGNYAASLLPGYEAKKRDFA
DVIYLDPATHTTIEEAGAANFFAITQDGQKFVTPQSPSILPSITKYSLLW
LAEHRLGLEVEEGDIRIDELGKFSEAGACGTAAVITPIGGIQHGDDFHVF
YSESEPGPVTRRLYDELVGIQYGDKEAPEGWIVKV
3D structure
PDB3uzb Crystal Structures of Complexes of the Branched-Chain Aminotransferase from Deinococcus radiodurans with alpha-Ketoisocaproate and L-Glutamate Suggest the Radiation Resistance of This Enzyme for Catalysis
ChainB
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K202
Catalytic site (residue number reindexed from 1) K179
Enzyme Commision number 2.6.1.42: branched-chain-amino-acid transaminase.
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 PLP B R100 K202 Y207 E238 A241 A242 L263 S265 I266 T267 G303 T304 R77 K179 Y184 E215 A218 A219 L240 S242 I243 T244 G280 T281
BS02 COI B Y143 Y175 A241 T304 A305 Y120 Y152 A218 T281 A282
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004084 branched-chain-amino-acid transaminase activity
GO:0008483 transaminase activity
GO:0052654 L-leucine-2-oxoglutarate transaminase activity
GO:0052655 L-valine-2-oxoglutarate transaminase activity
GO:0052656 L-isoleucine-2-oxoglutarate transaminase activity
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009081 branched-chain amino acid metabolic process
GO:0009082 branched-chain amino acid biosynthetic process
GO:0009097 isoleucine biosynthetic process
GO:0009098 L-leucine biosynthetic process
GO:0009099 L-valine biosynthetic process

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Molecular Function

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Biological Process
External links
PDB RCSB:3uzb, PDBe:3uzb, PDBj:3uzb
PDBsum3uzb
PubMed22984263
UniProtQ9RTX5

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