Research workbench

Damage-free as-isolated copper nitrite reductase from Bradyrhizobium sp. ORS 375 (two-domain) determined by serial femtosecond rotation crystallography

Analyse Damage-free as-isolated copper nitrite reductase from Bradyrhizobium sp. ORS… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ZAS
Type: protein
Length: 345 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.3
Source: Bradyrhizobium sp. (strain ORS 375)
Molecule: Copper-containing nitrite reductase
EC: 1.7.2.1
UniProt: H0SLX7
Ligands: CU, SO4
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · resolution 1.3 · 1 distinct chain · 11% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Copper-containing nitrite reductase (EC 1.7.2.1)	protein	345	11% helix, 39% strand	H0SLX7

Ligands and binding sites

CU · Copper (II) ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · 11 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.50	0.87	18	empty

Compared structures

6ZAS · Damage-free as-isolated copper nitrite reductase from bradyrhizobium sp. ors 375… · 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 H0SLX7
Elsewhere: RCSB PDB 6ZAS · PDBe 6ZAS · UniProt H0SLX7

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