MolNFT v1 · #164716 · protein

Glu-494-ala inactive monomer of a quinol dependent nitric oxide reductase (qnor) from alcaligenes xylosoxidans

6T6V · Nitric oxide reductase subunit B: “Glu-494-ala inactive monomer of a quinol dependent nitric oxide reductase (qnor) from alcaligenes xylosoxidans”. Electron microscopy, 2 ligands (HEM, CA), 12 pockets (best druggability 0.88).…

PDB: 6T6V
Type: protein
Length: 742 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nitric oxide reductase subunit B
EC: 1.7.2.5
UniProt: A0A0D6H8R3
Ligands: HEM, CA
Pockets: 12 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 60% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nitric oxide reductase subunit B (EC 1.7.2.5)	protein	742	60% helix, 2% strand	A0A0D6H8R3

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A
CA · Calcium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1068	0.88	0.89	107	HEM
2	300	0.76	0.88	46	empty
3	156	0.71	0.89	26	empty
4	61	0.65	0.93	14	empty
5	285	0.59	0.78	43	empty

Compared structures

6T6V · Glu-494-Ala inactive monomer of a quinol dependent Nitric Oxide Reductase (qNOR) from… · 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 A0A0D6H8R3
Elsewhere: RCSB PDB 6T6V · PDBe 6T6V · UniProt A0A0D6H8R3

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