MolNFT v1 · #84145 · protein

Structure of M92A variant of three-domain heme-cu nitrite reductase from ralstonia pickettii

3ZBM · Copper-containing nitrite reductase: “Structure of M92A variant of three-domain heme-cu nitrite reductase from ralstonia pickettii”. X-ray diffraction, 2 ligands (HEC, CU), 6 pockets (best druggability 0.76). MolNFT v1 #84145 on…

PDB: 3ZBM
Type: protein
Length: 455 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: E2STD2
Ligands: HEC, CU
Pockets: 6 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Copper-containing nitrite reductase (EC 1.7.2.1)	protein	455	21% helix, 33% strand	E2STD2

Ligands and binding sites

HEC · Heme C · ligand · chains A
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

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	225	0.76	0.90	35	HEC
2	284	0.58	0.77	34	empty
3	167	0.45	0.75	29	empty
4	69	0.43	0.81	21	empty
5	109	0.42	0.77	24	empty

Modifications

Observed in the structure: 2 cofactor (heme c attachment).

Compared structures

3ZBM · Structure of M92A variant of three-domain heme-Cu nitrite reductase from Ralstonia… · 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 E2STD2
Elsewhere: RCSB PDB 3ZBM · PDBe 3ZBM · UniProt E2STD2

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