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Crystal structures of the quinone oxidoreductase from thermus thermophilus HB8 and its complex with NADPH

Analyse Crystal structures of the quinone oxidoreductase from thermus thermophilus HB8… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IZ0
Type: protein
Length: 295 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Quinone oxidoreductase
EC: 1.6.5.5
UniProt: Q8L3C8
Ligands: SO4
Pockets: 2 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Quinone oxidoreductase (EC 1.6.5.5)	protein	295	33% helix, 31% strand	Q8L3C8

Ligands and binding sites

SO4 · Sulfate ion · ion · 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	666	0.75	0.80	58	SO4
2	69	0.37	0.78	15	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

1IZ0 · Crystal Structures of the Qui Oxidoreductase from Thermus thermophilus HB8 and Its… · 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 Q8L3C8
Elsewhere: RCSB PDB 1IZ0 · PDBe 1IZ0 · UniProt Q8L3C8

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