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Structure of the quinone oxidoreductase from coxiella burnetii

Analyse Structure of the quinone oxidoreductase from coxiella burnetii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TQH
Type: protein
Length: 317 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Quinone oxidoreductase
EC: 1.6.5.5
UniProt: Q83CT0
Ligands: NDP, SO4
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Quinone oxidoreductase (EC 1.6.5.5)	protein	317	34% helix, 28% strand	Q83CT0

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	574	0.76	0.82	53	NDP, SO4
2	171	0.46	0.76	30	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

3TQH · Structure of the qui oxidoreductase from Coxiella burnetii · 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 Q83CT0
Elsewhere: RCSB PDB 3TQH · PDBe 3TQH · UniProt Q83CT0

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