Structure of PDB 8c16 Chain D

Receptor sequence
>8c16D (length=327) Species: 226900 (Bacillus cereus ATCC 14579) [Search protein sequence]
ENQKVYDITIIGGGPTGLFTAFYGGMRQASVKIIESLPQLGGQLSALYPE
KYIYDVAGFPKVRAQELVDNLKEQMKKFDPTVCLEEAVDTLEKQADGIFK
LVTNKQTHYSKSVIITAGNGAFQPRRLELEGTAKYEKKNLHYFVDDMNKF
AGKRVVVFGGGDSAVDWTMMLEPIAEKVTIVHRRDKFRAHEHSVENLMNS
RAEVSTPYVPVELIGDDKIEQVVLQHVKTEEKVIIDVDDVIVNYGFVSSL
GPIKNWGLDIQKNSILVNSKMETNIPGIYAAGDICTYEGKVKLIACGFGE
APTAVNNAKAYFDPNAKLQPMVSSSMF
3D structure
PDB8c16 Functional Diversity of Homologous Oxidoreductases-Tuning of Substrate Specificity by a FAD-Stacking Residue for Iron Acquisition and Flavodoxin Reduction.
ChainD
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 D V326 S327 V322 S323
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

View graph for
Molecular Function

View graph for
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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