MolNFT v1 · #31961 · protein

Structural analysis of streptococcus pyogenes NADH oxidase: wild-type nox

2BC0: “Structural analysis of streptococcus pyogenes NADH oxidase: wild-type nox”. X-ray diffraction, 1 ligand (FAD), 8 pockets (best druggability 0.83). MolNFT v1 #31961 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2BC0
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: 8 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	NADH oxidase	protein	473	25% helix, 28% 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

8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	987	0.83	0.84	117	FAD
2	945	0.82	0.84	110	FAD
3	157	0.72	0.90	29	empty
4	150	0.69	0.89	31	empty
5	56	0.60	0.92	18	empty

Interfaces

1 interface between chains.

A–B · 3763 Å² buried · 28 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

2BC0 · Structural Analysis of Streptococcus pyogenes NADH oxidase: Wild-type 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 2BC0 · PDBe 2BC0 · UniProt Q1JLP2

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