Structure of PDB 5uxf Chain A

Receptor sequence
>5uxfA (length=316) Species: 10090 (Mus musculus) [Search protein sequence]
FQGMSSKQHCVKLNDGHLIPALGFGTYKPKEVPKSKSLEAACLALDVGYR
HVDTAYAYQVEEEIGQAIQSAIAAGVVKREDLFVTTKLWCTCFRPELVKP
ALEKSLKKLQLDYVDLYIMHYPVPMKSGDNDFPVNEQGKSLLDTVDFCDT
WERLEECKDAGLVKSIGVSNFNHRQLERILNKPGLKYKPVCNQVECHLYL
NQRKLLDYCESKDIVLVAYGALGTSPVLLNDPVLCDVAKKNKRSPALIAL
RYLIQRGIVPLAQSFKENEMRENLQVFGFQLSPEDMKTLDGLNKNFRYLP
AEFLVDHPEYPFVEEY
3D structure
PDB5uxf Sensing of Bacterial Cyclic Dinucleotides by the Oxidoreductase RECON Promotes NF-kappa B Activation and Shapes a Proinflammatory Antibacterial State.
ChainA
Resolution1.501 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D50 Y55 K84 H117
Catalytic site (residue number reindexed from 1) D53 Y58 K87 H120
Enzyme Commision number 1.1.1.-
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 2BA A Y24 G217 L219 T221 A253 Q270 S271 E276 N280 L306 Y27 G220 L222 T224 A246 Q263 S264 E269 N273 L299 MOAD: Kd=87nM
PDBbind-CN: -logKd/Ki=7.06,Kd=87nM
Gene Ontology
Molecular Function
GO:0004033 aldo-keto reductase (NADPH) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006805 xenobiotic metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5uxf, PDBe:5uxf, PDBj:5uxf
PDBsum5uxf
PubMed28329705
UniProtQ8VC28|AK1CD_MOUSE Aldo-keto reductase family 1 member C13 (Gene Name=Akr1c13)

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