MolNFT v1 · #38721 · protein

Crystal structure of thioredoxin mutant E85D in hexagonal (P61) space group

2H72: “Crystal structure of thioredoxin mutant E85D in hexagonal (P61) space group”. X-ray diffraction, 3 pockets (best druggability 0.41). MolNFT v1 #38721 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2H72
Type: protein
Length: 214 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin
UniProt: Q2M889
Pockets: 3 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin	protein	107	34% helix, 26% strand	Q2M889
B	Thioredoxin	protein	107	35% helix, 23% strand	Q2M889

Ligands and binding sites

MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, B

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	76	0.41	0.79	20	empty
2	64	0.33	0.75	15	empty
3	66	0.31	0.75	14	MPD

Interfaces

1 interface between chains.

A–B · 514 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2H72 · Crystal Structure of Thioredoxin mutant E85D 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 2H72 · PDBe 2H72 · UniProt Q2M889

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