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Solution structure of the DNA binding domain of human TRF1

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

PDB: 1ITY
Type: protein
Length: 67 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRF1
UniProt: P54274
Pockets: 1 · best druggability 0.32

Structure

solution nmr · 1 distinct chain · 51% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TRF1	protein	67	51% helix, 0% strand	P54274

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	82	0.32	0.74	17	empty

Compared structures

1ITY · Solution structure of the DNA binding domain of 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 0.76

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 1ITY · PDBe 1ITY · UniProt P54274

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