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The structure of the arabidopsis thaliana TOC75 potra domains

Analyse The structure of the arabidopsis thaliana TOC75 potra domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UBC
Type: protein
Length: 600 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein TOC75-3, chloroplastic
UniProt: Q9STE8
Pockets: 7 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein TOC75-3, chloroplastic	protein	300	30% helix, 27% strand	Q9STE8

Pockets

7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	341	0.64	0.80	34	empty
2	87	0.63	0.90	22	empty
3	91	0.61	0.88	22	empty
4	236	0.56	0.78	24	empty
5	249	0.54	0.77	25	empty

Interfaces

1 interface between chains.

A–B · 438 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

5UBC · The structure of the Arabidopsis thaliana Toc75 POTRA domains · the same entry in another collection · chain A against A, TM-score 1.00
Q9STE8 · AlphaFold monomer V2.0 prediction for protein TOC75-3, chloroplastic (Q9STE8) · a predicted model of the same protein · chain A against A, TM-score 0.85

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 Q9STE8
Elsewhere: RCSB PDB 5UBC · PDBe 5UBC · UniProt Q9STE8

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