Research workbench

Crystal structure of the H286L mutant of ferredoxin-NADP+ reductase from plasmodium falciparum

Analyse Crystal structure of the H286L mutant of ferredoxin-NADP+ reductase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3JQR
Type: protein
Length: 256 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ferredoxin NADP reductase
EC: 1.18.1.2
UniProt: C6KT68
Ligands: FAD
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferredoxin NADP reductase (EC 1.18.1.2)	protein	256	29% helix, 28% strand	C6KT68

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	361	0.65	0.79	41	FAD
2	51	0.30	0.76	11	empty

Compared structures

3JQR · Crystal structure of the H286L mutant of Ferredoxin-NADP+ reductase from Plasmodium… · the same entry in another collection · chain A against A, TM-score 1.00
C6KT68 · AlphaFold monomer V2.0 prediction for ferredoxin--NADP reductase, apicoplast (C6KT68) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 C6KT68
Elsewhere: RCSB PDB 3JQR · PDBe 3JQR · UniProt C6KT68

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.