MolNFT v1 · #8691 · protein

FERREDOXIN:NADP+ reductase mutant with val 136 replaced by leu (V136L)

1H85 · Ferredoxin--NADP reductase: “FERREDOXIN:NADP+ reductase mutant with val 136 replaced by leu (V136L)”. X-ray diffraction, 2 ligands (FAD, SO4), 2 pockets (best druggability 0.52). MolNFT v1 #8691 on GenesisL1: 3D structure, binding…

PDB: 1H85
Type: protein
Length: 295 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: P21890
Ligands: FAD, SO4
Pockets: 2 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferredoxin--NADP reductase (EC 1.18.1.2)	protein	295	27% helix, 29% strand	P21890

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
SO4 · Sulfate ion · ion · 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	217	0.52	0.77	29	SO4
2	163	0.50	0.78	25	FAD

Compared structures

1H85 · FERREDOXIN:NADP+ reductase mutant with val 136 replaced by leu (V136L) · the same entry in another collection · chain A against A, TM-score 1.00
P21890 · AlphaFold monomer V2.0 prediction for ferredoxin--NADP reductase (P21890) · 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 P21890
Elsewhere: RCSB PDB 1H85 · PDBe 1H85 · UniProt P21890

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