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Crystal structure of TRF2 trfh in complex with an NBS1 peptide

Analyse Crystal structure of TRF2 trfh in complex with an NBS1 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WQD
Type: protein
Length: 1,470 residues
Chains: 14
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Telomeric repeat-binding factor 2; Nibrin
UniProt: Q15554, O60934
Pockets: 20 · best druggability 0.78

Structure

x-ray diffraction · 12 distinct chains · 68% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Telomeric repeat-binding factor 2	protein	202	72% helix, 1% strand	Q15554
B	Telomeric repeat-binding factor 2	protein	202	71% helix, 1% strand	Q15554
C	Telomeric repeat-binding factor 2	protein	204	72% helix, 1% strand	Q15554
D	Telomeric repeat-binding factor 2	protein	203	72% helix, 2% strand	Q15554
E	Telomeric repeat-binding factor 2	protein	198	71% helix, 0% strand	Q15554
F	Telomeric repeat-binding factor 2	protein	195	70% helix, 1% strand	Q15554
G	Telomeric repeat-binding factor 2	protein	195	66% helix, 1% strand	Q15554
H	Nibrin	protein	12	0% helix, 17% strand	O60934
I	Nibrin	protein	13	0% helix, 15% strand	O60934
J, K, L	Nibrin	protein	10	0% helix, 20% strand	O60934
M	Nibrin	protein	7	0% helix, 14% strand	O60934
N	Nibrin	protein	9	0% helix, 11% strand	O60934

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	954	0.78	0.80	99	empty
2	674	0.70	0.78	43	empty
3	420	0.58	0.75	37	empty
4	143	0.53	0.81	18	empty
5	162	0.52	0.79	23	empty

Interfaces

20 interfaces between chains.

A–B · 1353 Å² buried · 6 hydrogen bonds · protein-protein
C–D · 1301 Å² buried · 7 hydrogen bonds · protein-protein
E–F · 1170 Å² buried · 6 hydrogen bonds · protein-protein
A–H · 856 Å² buried · 12 hydrogen bonds · protein-protein
B–I · 715 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

5WQD · Crystal structure of TRF2 TRFH in complex with an NBS1 peptide · the same entry in another collection · chain M against M, TM-score 1.00

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
Every structure of UniProt O60934
Elsewhere: RCSB PDB 5WQD · PDBe 5WQD · UniProt Q15554 · UniProt O60934

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