Research workbench

Crystal structure of the pin domain of human EST1A

Analyse Crystal structure of the pin domain of human EST1A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2DOK
Type: protein
Length: 338 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Telomerase-binding protein EST1A
UniProt: Q86US8
Pockets: 3 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Telomerase-binding protein EST1A	protein	170	48% helix, 19% strand	Q86US8
B	Telomerase-binding protein EST1A	protein	168	49% helix, 21% strand	Q86US8

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	154	0.53	0.80	27	empty
2	97	0.38	0.76	20	empty
3	79	0.32	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 555 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2DOK · Crystal structure of the PIN domain of human EST1A · the same entry in another collection · chain A against A, TM-score 1.00
Q86US8 · AlphaFold monomer V2.0 prediction for telomerase-binding protein EST1A (Q86US8) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q86US8
Elsewhere: RCSB PDB 2DOK · PDBe 2DOK · UniProt Q86US8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.