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Crystal structure analysis of the ferredoxin-NADP+ reductase from maize leaf

Analyse Crystal structure analysis of the ferredoxin-NADP+ reductase from maize leaf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GAW
Type
protein
Length
609 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferredoxin-NADP+ reductase
EC
1.18.1.2
UniProt
Q9SLP6
Ligands
FAD
Pockets
3 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFerredoxin-NADP+ reductase (EC 1.18.1.2)protein30425% helix, 30% strandQ9SLP6
BFerredoxin-NADP+ reductase (EC 1.18.1.2)protein30525% helix, 30% strandQ9SLP6

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15060.590.7453empty
22770.570.7743FAD
32590.570.7843FAD

Interfaces

1 interface between chains.

  • A–B · 363 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1GAW · Crystal structure analysis of the ferredoxin-NADP+ reductase from maize leaf · the same entry in another collection · chain A against A, TM-score 1.00

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