MolNFT v1 · #149297 · protein

Low resolution structure of neisseria meningitidis qnor

6FWF · Nitric-oxide reductase: “Low resolution structure of neisseria meningitidis qnor”. X-ray diffraction, 3 ligands (HEM, CA, FE), 8 pockets (best druggability 0.88). MolNFT v1 #149297 on GenesisL1: 3D structure, binding sites and…

PDB: 6FWF
Type: protein
Length: 712 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nitric-oxide reductase
EC: 1.7.99.7
UniProt: C6S880
Ligands: HEM, CA, FE
Pockets: 8 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nitric-oxide reductase (EC 1.7.99.7)	protein	712	64% helix, 2% strand	C6S880

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A
CA · Calcium ion · metal · chains A
FE · Fe (III) ion · metal · chains A

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

Pockets

8 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	677	0.88	0.92	83	HEM
2	1026	0.77	0.79	110	empty
3	99	0.74	0.95	31	empty
4	81	0.63	0.90	18	empty
5	134	0.58	0.84	23	empty

Compared structures

6FWF · Low resolution structure of Neisseria meningitidis qNOR · 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 C6S880
Elsewhere: RCSB PDB 6FWF · PDBe 6FWF · UniProt C6S880

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