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Structure of the C-terminal domain of human telomeric STN1

Analyse Structure of the C-terminal domain of human telomeric STN1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4JQF
Type: protein
Length: 168 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cst complex subunit STN1
UniProt: Q9H668

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cst complex subunit STN1	protein	168	60% helix, 12% strand	Q9H668

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4JQF · Structure of the C-terminal domain of human telomeric Stn1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9H668 · AlphaFold monomer V2.0 prediction for cst complex subunit STN1 (Q9H668) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9H668
Elsewhere: RCSB PDB 4JQF · PDBe 4JQF · UniProt Q9H668

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