Structure of PDB 5ygq Chain B

Receptor sequence
>5ygqB (length=340) Species: 258594 (Rhodopseudomonas palustris CGA009) [Search protein sequence]
ETIKTDVLIVGAGPCGLFAVFELGLLDVKAHLVDILDKVGGQCAELYPEK
PIYDIPGIPMVTGHGLTEALMEQIKPFNPTFHLSEMVENVEKIGDPGFRV
TTNAGKVFECTVLVVAAGGGSFLPKRPPVPGVEAYEGTSVHYAVRKMEDF
RGKDILIVGGGDSALDWTLNLNPIAKSMTLVHRRDDFRGAPHSVEQMRQL
VASGKLDLKIGQITELQGDNGQLTGATVKLNDNTTSQIKCDAMLPFFGLT
MKLGPVANWGLDLENNLIPVDTGTFETNVPGIFAIGDINTYPGKLKLILS
GFHEGALMAQKAVKYVYPDKRVVFQYTTSSTNLQKKLGVN
3D structure
PDB5ygq Kinetic and structural insight into a role of the re-face Tyr328 residue of the homodimer type ferredoxin-NADP+oxidoreductase from Rhodopseudomonas palustris in the reaction with NADP+/NADPH.
ChainB
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.18.1.2: ferredoxin--NADP(+) reductase.
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 FAD B Y328 T330 Y326 T328
BS02 FAD B V12 G13 G15 P16 C17 D36 I37 Q44 Y49 D56 M88 V89 A119 G120 G122 S123 F124 D289 L299 I300 V10 G11 G13 P14 C15 D34 I35 Q42 Y47 D54 M86 V87 A117 G118 G120 S121 F122 D287 L297 I298
Gene Ontology
Molecular Function
GO:0004324 ferredoxin-NADP+ reductase activity
GO:0004791 thioredoxin-disulfide reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0050661 NADP binding
Biological Process
GO:0045454 cell redox homeostasis
GO:0098869 cellular oxidant detoxification

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Molecular Function
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Biological Process
External links
PDB RCSB:5ygq, PDBe:5ygq, PDBj:5ygq
PDBsum5ygq
PubMed31838096
UniProtQ6N2U4|FENR_RHOPA Ferredoxin--NADP reductase (Gene Name=RPA3954)

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