Research workbench

MET150LEU/PHE312CYS variant of nitrite reductase from alcaligenes faecalis

Analyse MET150LEU/PHE312CYS variant of nitrite reductase from alcaligenes faecalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3H56
Type: protein
Length: 336 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: P38501
Ligands: CU
Pockets: 3 · best druggability 0.72

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	336	11% helix, 39% strand	P38501

Ligands and binding sites

CU · Copper (II) ion · metal · 2 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	61	0.72	0.97	18	empty
2	50	0.49	0.87	16	empty
3	67	0.29	0.73	24	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

3H56 · Met150Leu/Phe312Cys variant of nitrite reductase from Alcaligenes faecalis · 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 P38501
Elsewhere: RCSB PDB 3H56 · PDBe 3H56 · UniProt P38501

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