MolNFT v1 · #109483 · protein

Structure of proline-free E. COLI thioredoxin

4X43 · Thioredoxin-1: “Structure of proline-free E. COLI thioredoxin”. X-ray diffraction, 1 pocket (best druggability 0.48). MolNFT v1 #109483 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4X43
Type: protein
Length: 321 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin-1
UniProt: P0AA25
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 3 distinct chains · 36% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin-1	protein	106	37% helix, 27% strand	P0AA25
B	Thioredoxin-1	protein	108	34% helix, 27% strand	P0AA25
C	Thioredoxin-1	protein	107	37% helix, 25% strand	P0AA25

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	176	0.48	0.76	25	empty

Interfaces

2 interfaces between chains.

A–B · 671 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 491 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

4X43 · Structure of proline-free E. coli Thioredoxin · the same entry in another collection · chain A against A, TM-score 1.00
P0AA25 · AlphaFold monomer V2.0 prediction for thioredoxin 1 (P0AA25) · a predicted model of the same protein · chain C against A, TM-score 0.96

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 P0AA25
Elsewhere: RCSB PDB 4X43 · PDBe 4X43 · UniProt P0AA25

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