Research workbench

Achromobacter cycloclastes copper nitrite reductase at pH 5.5

Analyse Achromobacter cycloclastes copper nitrite reductase at pH 5.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GTK
Type: protein
Length: 333 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Copper-containing nitrite reductase
EC: 1.7.2.1
UniProt: P25006
Ligands: CU, NO2
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Copper-containing nitrite reductase (EC 1.7.2.1)	protein	333	11% helix, 40% strand	P25006

Ligands and binding sites

CU · Copper (II) ion · metal · 2 copies · chains A
NO2 · Nitrite ion · ion · chains A
MLI · Malonate ion · additive · 2 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	187	0.75	0.91	26	empty

Compared structures

6GTK · Achromobacter cycloclastes copper nitrite reductase at pH 5.5 · the same entry in another collection · chain A against A, TM-score 1.00
P25006 · AlphaFold monomer V2.0 prediction for copper-containing nitrite reductase (P25006) · a predicted model of the same protein · 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 P25006
Elsewhere: RCSB PDB 6GTK · PDBe 6GTK · UniProt P25006

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