Research workbench

Crystal structure of a Ferredoxin-Flavin Thioredoxin Reductase from Clostridium acetobutylicum at 1.64 A resolution

Analyse Crystal structure of a Ferredoxin-Flavin Thioredoxin Reductase from Clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GNC
Type: protein
Length: 287 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.639
Source: Clostridium acetobutylicum ATCC 824
Molecule: Thioredoxin reductase
UniProt: Q97IU2
Ligands: FAD
Pockets: 4 · best druggability 0.75

Structure

x-ray diffraction · resolution 1.639 · 1 distinct chain · 27% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin reductase	protein	287	27% helix, 27% strand	Q97IU2

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	593	0.75	0.82	58	FAD, PEG
2	140	0.52	0.80	23	empty
3	68	0.37	0.78	14	empty
4	73	0.31	0.74	15	empty

Compared structures

6GNC · Crystal structure of a ferredoxin-flavin thioredoxin reductase from clostridium… · 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 Q97IU2
Elsewhere: RCSB PDB 6GNC · PDBe 6GNC · UniProt Q97IU2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.