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Dimerisation domain from human TRF1

Analyse Dimerisation domain from human TRF1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H6O
Type: protein
Length: 195 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Telomeric repeat binding factor 1
UniProt: P54274
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Telomeric repeat binding factor 1	protein	195	68% helix, 0% strand	P54274

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	99	0.55	0.84	17	empty
2	97	0.37	0.75	23	empty

Compared structures

1H6O · Dimerisation domain from human TRF1 · the same entry in another collection · chain A against A, TM-score 1.00
P54274 · AlphaFold monomer V2.0 prediction for telomeric repeat-binding factor 1 (P54274) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P54274
Elsewhere: RCSB PDB 1H6O · PDBe 1H6O · UniProt P54274

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