MolNFT v1 · #25091 · protein + DNA

Solution structure of the DNA complex of human TRF2

1VFC · Short G-rich strand: “Solution structure of the DNA complex of human TRF2”. Solution nmr, 1 pocket (best druggability 0.49). MolNFT v1 #25091 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1VFC
Type: protein + DNA
Length: 89 residues
Chains: 3
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Short G-rich strand; Short C-rich starnd; Telomeric repeat binding factor 2
UniProt: Q15554
Pockets: 1 · best druggability 0.49

Structure

solution nmr · 3 distinct chains · 52% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Short G-rich strand	dna	13	—	—
C	Short C-rich starnd	dna	13	—	—
A	Telomeric repeat binding factor 2	protein	63	52% helix, 0% strand	Q15554

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	126	0.49	0.80	15	empty

Interfaces

3 interfaces between chains.

B–C · 583 Å² buried · 43 hydrogen bonds · nucleic-nucleic
C–A · 487 Å² buried · 7 hydrogen bonds · protein-nucleic
B–A · 487 Å² buried · 11 hydrogen bonds · protein-nucleic

Compared structures

1VFC · Solution Structure Of The DNA Complex Of Human Trf2 · the same entry in another collection · chain B against B, TM-score 1.00
Q15554 · AlphaFold monomer V2.0 prediction for telomeric repeat-binding factor 2 (Q15554) · a predicted model of the same protein · chain A against A, TM-score 0.74

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 Q15554
Elsewhere: RCSB PDB 1VFC · PDBe 1VFC · UniProt Q15554

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