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Crystal Structure of Thioredoxin Mutant E48D in Hexagonal (p61) Space Group

Analyse Crystal Structure of Thioredoxin Mutant E48D in Hexagonal (p61) Space Group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2H6Y
Type: protein
Length: 214 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.4
Source: Escherichia coli
Molecule: Thioredoxin
UniProt: Q2M889
Pockets: 3 · best druggability 0.41

Structure

x-ray diffraction · resolution 2.4 · 1 distinct chain · 36% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Thioredoxin	protein	107	36% helix, 26% strand	Q2M889

Ligands and binding sites

MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	85	0.41	0.78	17	empty
2	82	0.38	0.76	15	empty
3	77	0.34	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 517 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2H6Y · Crystal structure of thioredoxin mutant E48D in hexagonal (P61) space group · 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 Q2M889
Elsewhere: RCSB PDB 2H6Y · PDBe 2H6Y · UniProt Q2M889

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