MolNFT v1 · #19285 · protein

Wild-type pea fnr

1QG0 · Protein (FERREDOXIN:NADP+ reductase): “Wild-type pea fnr”. X-ray diffraction, 1 ligand (FAD), 3 pockets (best druggability 0.68). MolNFT v1 #19285 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1QG0
Type: protein
Length: 592 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (FERREDOXIN:NADP+ reductase)
EC: 1.18.1.2
UniProt: P10933
Ligands: FAD
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein (FERREDOXIN:NADP+ reductase) (EC 1.18.1.2)	protein	296	25% helix, 31% strand	P10933

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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	437	0.68	0.79	49	FAD
2	402	0.65	0.78	48	FAD
3	71	0.27	0.72	15	empty

Interfaces

1 interface between chains.

A–B · 477 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

1QG0 · Wild-type pea fnr · 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

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P10933
Elsewhere: RCSB PDB 1QG0 · PDBe 1QG0 · UniProt P10933

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