Research workbench

Crystal structure of a putative NADPH:QUINONE reductase (MLL3093) from mesorhizobium loti at 1.71 a resolution

Analyse Crystal structure of a putative NADPH:QUINONE reductase (MLL3093) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PI7
Type: protein
Length: 344 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NADH oxidoreductase
UniProt: Q98H03
Ligands: K, PO4
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NADH oxidoreductase	protein	344	35% helix, 24% strand	Q98H03

Ligands and binding sites

K · Potassium ion · metal · chains A
PO4 · Phosphate ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

3 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	1022	0.80	0.81	76	empty
2	101	0.39	0.76	19	empty
3	50	0.30	0.76	16	empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

3PI7 · Crystal structure of a putative NADPH:qui reductase (mll3093) from Mesorhizobium loti at… · the same entry in another collection · chain A against A, TM-score 1.00

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 Q98H03
Elsewhere: RCSB PDB 3PI7 · PDBe 3PI7 · UniProt Q98H03

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