MolNFT v1 · #39534 · protein

Structure of pin domain of human SMG6

2HWW · Telomerase-binding protein EST1A: “Structure of pin domain of human SMG6”. X-ray diffraction, 2 pockets (best druggability 0.55). MolNFT v1 #39534 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2HWW
Type: protein
Length: 461 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Telomerase-binding protein EST1A
UniProt: Q86US8
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 3 distinct chains · 49% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Telomerase-binding protein EST1A	protein	160	51% helix, 19% strand	Q86US8
B	Telomerase-binding protein EST1A	protein	157	49% helix, 20% strand	Q86US8
C	Telomerase-binding protein EST1A	protein	144	47% helix, 22% strand	Q86US8

Pockets

2 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	78	0.55	0.86	27	empty
2	100	0.49	0.81	14	empty

Interfaces

2 interfaces between chains.

A–B · 958 Å² buried · 13 hydrogen bonds · protein-protein
B–C · 670 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

2HWW · Structure of PIN domain of human SMG6 · 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 B 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 Q86US8
Elsewhere: RCSB PDB 2HWW · PDBe 2HWW · UniProt Q86US8

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