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Crystal structure of the myb domain of S. pombe TBF1

Analyse Crystal structure of the myb domain of S. pombe TBF1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6K5U
Type: protein
Length: 156 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Telomeric DNA-binding factor TRF1
UniProt: Q6E434
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Telomeric DNA-binding factor TRF1	protein	77	56% helix, 0% strand	Q6E434
B	Telomeric DNA-binding factor TRF1	protein	79	56% helix, 0% strand	Q6E434

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	61	0.29	0.73	12	empty

Interfaces

1 interface between chains.

A–B · 427 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

6K5U · Crystal structure of the myb domain of S. pombe Tbf1 · the same entry in another collection · chain A against A, TM-score 1.00
Q6E434 · AlphaFold monomer V2.0 prediction for telomeric DNA-binding factor TRF1 (Q6E434) · 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 Q6E434
Elsewhere: RCSB PDB 6K5U · PDBe 6K5U · UniProt Q6E434

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