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The structure of the axh domain of ataxin-1.

Analyse The structure of the axh domain of ataxin-1. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4APT
Type: protein
Length: 499 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ataxin-1
UniProt: P54253
Ligands: NA
Pockets: 9 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Ataxin-1	protein	125	18% helix, 42% strand	P54253
D	Ataxin-1	protein	124	22% helix, 39% strand	P54253

Ligands and binding sites

NA · Sodium ion · metal · chains D

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

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	91	0.77	0.98	23	empty
2	75	0.75	0.98	21	empty
3	66	0.74	0.98	25	empty
4	554	0.70	0.79	56	empty
5	216	0.59	0.80	30	empty

Interfaces

3 interfaces between chains.

A–B · 1757 Å² buried · 4 hydrogen bonds · protein-protein
C–D · 1681 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 723 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

4APT · The structure of the AXH domain of ataxin-1. · the same entry in another collection · chain D against D, TM-score 1.00
P54253 · AlphaFold monomer V2.0 prediction for ataxin-1 (P54253) · a predicted model of the same protein · chain C against A, TM-score 0.94

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 P54253
Elsewhere: RCSB PDB 4APT · PDBe 4APT · UniProt P54253

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