MolNFT v1 · #31962 · protein

Structural analysis of streptococcus pyogenes NADH oxidase: C44S nox

2BC1: “Structural analysis of streptococcus pyogenes NADH oxidase: C44S nox”. X-ray diffraction, 1 ligand (FAD), 9 pockets (best druggability 0.83). MolNFT v1 #31962 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2BC1
Type: protein
Length: 946 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NADH oxidase
UniProt: Q1JLP2
Ligands: FAD
Pockets: 9 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	NADH oxidase	protein	473	25% helix, 29% strand	Q1JLP2

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1034	0.83	0.84	114	FAD
2	507	0.82	0.89	68	FAD
3	129	0.72	0.91	31	empty
4	137	0.71	0.90	31	empty
5	457	0.67	0.79	50	empty

Interfaces

1 interface between chains.

A–B · 3857 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

2BC1 · Structural Analysis of Streptococcus pyogenes NADH oxidase: C44S Nox · 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 Q1JLP2
Elsewhere: RCSB PDB 2BC1 · PDBe 2BC1 · UniProt Q1JLP2

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