Research workbench

E. COLI thioredoxin variant with (4R)-FLUOROPRO76 as single proline residue

Analyse E. COLI thioredoxin variant with (4R)-FLUOROPRO76 as single proline residue in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HUA
Type: protein
Length: 108 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin-1
UniProt: P0AA25
Ligands: CU
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin-1	protein	108	34% helix, 28% strand	P0AA25

Ligands and binding sites

CU · Copper (II) ion · metal · chains A

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

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	62	0.35	0.77	12	empty

Modifications

Observed in the structure: 1 disulfide, 1 modified (disulfide, nonstandard).

Compared structures

4HUA · E. coli thioredoxin variant with (4R)-FluoroPro76 as single proline residue · 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 A against A, TM-score 0.97

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 4HUA · PDBe 4HUA · UniProt P0AA25

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