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Crystal structure of an engineered ferredoxin NADP reductase (fnr) from pisum sativum

Analyse Crystal structure of an engineered ferredoxin NADP reductase (fnr) from pisum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2XNC
Type
protein
Length
575 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferredoxin--NADP reductase, leaf isozyme, chloroplastic
EC
1.18.1.2
UniProt
P10933
Ligands
FAD, SO4
Pockets
8 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFerredoxin--NADP reductase, leaf isozyme, chloroplastic (EC 1.18.1.2)protein28726% helix, 29% strandP10933
BFerredoxin--NADP reductase, leaf isozyme, chloroplastic (EC 1.18.1.2)protein28825% helix, 30% strandP10933

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14440.610.7548empty
21750.530.7923empty
31790.500.7727empty
41640.490.7728FAD
51390.450.7626FAD

Interfaces

1 interface between chains.

  • A–B · 410 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 2XNC · Crystal structure of an engineered Ferredoxin NADP reductase (FNR) from Pisum sativum · the same entry in another collection · chain A against A, TM-score 1.00
  • P10933 · AlphaFold monomer V2.0 prediction for ferredoxin--NADP reductase, leaf isozyme… · a predicted model of the same protein · chain A against A, TM-score 0.99

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