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Structure of human thioredoxin 2

Analyse Structure of human thioredoxin 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UVZ
Type: protein
Length: 654 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin
UniProt: Q99757
Pockets: 4 · best druggability 0.66

Structure

x-ray diffraction · 4 distinct chains · 39% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, E	Thioredoxin	protein	110	37% helix, 25% strand	Q99757
C	Thioredoxin	protein	107	42% helix, 26% strand	Q99757
D	Thioredoxin	protein	109	38% helix, 26% strand	Q99757
F	Thioredoxin	protein	108	40% helix, 26% strand	Q99757

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	584	0.66	0.76	66	empty
2	512	0.64	0.76	65	empty
3	62	0.29	0.74	13	empty
4	54	0.28	0.74	15	empty

Interfaces

9 interfaces between chains.

C–D · 495 Å² buried · 4 hydrogen bonds · protein-protein
E–F · 494 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 487 Å² buried · 5 hydrogen bonds · protein-protein
A–D · 412 Å² buried · 9 hydrogen bonds · protein-protein
B–E · 405 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

1UVZ · structure of human thioredoxin 2 · the same entry in another collection · chain F against F, TM-score 1.00
Q99757 · AlphaFold monomer V2.0 prediction for thioredoxin, mitochondrial (Q99757) · a predicted model of the same protein · chain C against A, TM-score 0.99

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 Q99757
Elsewhere: RCSB PDB 1UVZ · PDBe 1UVZ · UniProt Q99757

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