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As-isolated resting state copper nitrite reductase from achromobacter xylosoxidans

Analyse As-isolated resting state copper nitrite reductase from achromobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ONY
Type: protein
Length: 335 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: O68601
Ligands: CU, ZN
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 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	335	11% helix, 39% strand	O68601

Ligands and binding sites

CU · Copper (II) ion · metal · 2 copies · chains A
ZN · Zinc ion · metal · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A
PG4 · Tetraethylene glycol · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	85	0.39	0.77	17	empty

Compared structures

5ONY · As-isolated resting state copper nitrite reductase from Achromobacter xylosoxidans · 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 O68601
Elsewhere: RCSB PDB 5ONY · PDBe 5ONY · UniProt O68601

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