Structure of PDB 8upp Chain F

Receptor sequence
>8uppF (length=327) Species: 197 (Campylobacter jejuni) [Search protein sequence]
ITVYYDKDCDLNLIKSKKVAIIGFGSQGHAHAMNLRDNGVNVTIGLREGS
VSAVKAKNAGFEVMSVSEASKIADVIMILAPDEIQADIFNVEIKPNLSEG
KAIAFAHGFNIHYGQIVVPKGVDVIMIAPKAPGHTVRNEFTLGGGTPCLI
AIHQDESKNAKNLALSYASAIGGGRTGIIETTFKAETETDLFGEQAVLCG
GLSALIQAGFETLVEAGYEPEMAYFECLHEMKLIVDLIYQGGIADMRYSI
SNTAEYGDYITGPKIITEETKKAMKGVLKDIQNGVFAKDFILERRAGFAR
MHAERKNMNDSLIEKTGRNLRAMMPWI
3D structure
PDB8upp Mapping of the Reaction Trajectory catalyzed by Class I Ketol-Acid Reductoisomerase
ChainF
Resolution1.78 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.86: ketol-acid reductoisomerase (NADP(+)).
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 NDP F I252 S253 I250 S251
BS02 X9W F A133 P134 D192 E196 A131 P132 D190 E194
BS03 X9W F E232 I252 S253 A256 E230 I250 S251 A254
BS04 MG F D192 E196 D190 E194
BS05 NDP F F26 G27 S28 Q29 R49 S54 L81 A82 P83 D84 I90 H109 F24 G25 S26 Q27 R47 S52 L79 A80 P81 D82 I88 H107
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004455 ketol-acid reductoisomerase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050661 NADP binding
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009082 branched-chain amino acid biosynthetic process
GO:0009097 isoleucine biosynthetic process
GO:0009099 L-valine biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:8upp, PDBe:8upp, PDBj:8upp
PDBsum8upp
PubMed
UniProtQ9PHN5|ILVC_CAMJE Ketol-acid reductoisomerase (NADP(+)) (Gene Name=ilvC)

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