Structure of PDB 8c16 Chain A

Receptor sequence
>8c16A (length=314) Species: 226900 (Bacillus cereus ATCC 14579) [Search protein sequence]
NQKVYDITIIGGGPTGLFTAFYGGMRQASVKIIESLPQLGGQLSALYPEK
YIYDVAGFPKVRAQELVDNLKEQMKKFDPTVCLEEAVDTLEKQADGIFKL
VTNKQTHYSKSVIITAGNGAFQPRRLELEGTAKYEKKNLHYFVDDMNKFA
GKRVVVFGGGDSAVDWTMMLEPIAEKVTIVHRRDKFRAHEHSVENLMNSR
AEVSTPYVPVELIGDDKIEQVVLQHVKTEEKVIIDVDDVIVNYGFVSSLG
PIKNWGLDIQKNSILVNSKMETNIPGIYAAGDICTYEGKVKLIACGFGEA
PTAVNNAKAYFDPN
3D structure
PDB8c16 Functional Diversity of Homologous Oxidoreductases-Tuning of Substrate Specificity by a FAD-Stacking Residue for Iron Acquisition and Flavodoxin Reduction.
ChainA
Resolution4.2 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 A G16 G18 P19 E39 S40 G46 Q47 Y52 I57 D59 A91 V92 A121 G122 G124 A125 F126 D287 L297 I298 G11 G13 P14 E34 S35 G41 Q42 Y47 I52 D54 A86 V87 A116 G117 G119 A120 F121 D282 L292 I293
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:8c16, PDBe:8c16, PDBj:8c16
PDBsum8c16
PubMed37371954
UniProtQ816D9|FENR_BACCR Ferredoxin--NADP reductase (Gene Name=BC_4926)

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