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Crystal structure of nitrite reductase ASP98ASN mutant from alcaligenes faecalis S-6

Analyse Crystal structure of nitrite reductase ASP98ASN mutant from alcaligenes… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ET5
Type: protein
Length: 336 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nitrite reductase
EC: 1.7.99.3
UniProt: P38501
Ligands: CU, ZN
Pockets: 2 · best druggability 0.71

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nitrite reductase (EC 1.7.99.3)	protein	336	11% helix, 40% strand	P38501

Ligands and binding sites

CU · Copper (II) ion · metal · 2 copies · chains A
ZN · Zinc ion · metal · 2 copies · 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	56	0.71	0.98	18	empty
2	76	0.44	0.81	17	empty

Compared structures

1ET5 · Crystal structure of nitrite reductase ASP98ASN mutant from alcaligenes faecalis S-6 · the same entry in another collection · chain A against A, TM-score 1.00
P38501 · AlphaFold monomer V2.0 prediction for copper-containing nitrite reductase (P38501) · 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 P38501
Elsewhere: RCSB PDB 1ET5 · PDBe 1ET5 · UniProt P38501

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