Structure of PDB 6gas Chain D

Receptor sequence
>6gasD (length=326) Species: 226900 (Bacillus cereus ATCC 14579) [Search protein sequence]
NQKVYDITIIGGGPTGLFTAFYGGMRQASVKIIESLPQLGGQLSALYPEK
YIYDVAGFPKVRAQELVDNLKEQMKKFDPTVCLEEAVDTLEKQADGIFKL
VTNKQTHYSKSVIITAGNGAFQPRRLELEGTAKYEKKNLHYFVDDMNKFA
GKRVVVFGGGDSAVDWTMMLEPIAEKVTIVHRRDKFRAHEHSVENLMNSR
AEVSTPYVPVELIGDDKIEQVVLQHVKTEEKVIIDVDDVIVNYGFVSSLG
PIKNWGLDIQKNSILVNSKMETNIPGIYAAGDICTYEGKVKLIACGFGEA
PTAVNNAKAYFDPNAKLQPMHSSSMF
3D structure
PDB6gas The Characterization of Different Flavodoxin Reductase-Flavodoxin (FNR-Fld) Interactions Reveals an Efficient FNR-Fld Redox Pair and Identifies a Novel FNR Subclass.
ChainD
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 D H326 S327 H321 S322
BS02 FAD D I15 G16 G18 P19 T20 E39 S40 G46 Q47 L48 Y52 D59 A91 V92 A121 G122 G124 A125 D287 L297 I298 I10 G11 G13 P14 T15 E34 S35 G41 Q42 L43 Y47 D54 A86 V87 A116 G117 G119 A120 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:6gas, PDBe:6gas, PDBj:6gas
PDBsum6gas
PubMed30142264
UniProtQ816D9|FENR_BACCR Ferredoxin--NADP reductase (Gene Name=BC_4926)

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