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Structural basis for shelterin bridge assembly

Analyse Structural basis for shelterin bridge assembly in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WE0
Type: protein
Length: 1,057 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protection of telomeres protein POZ1; Protection of telomeres protein TPZ1; DNA-binding…
UniProt: O13852, O14246, Q96TL7
Ligands: ZN
Pockets: 7 · best druggability 0.66

Structure

x-ray diffraction · 9 distinct chains · 69% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protection of telomeres protein POZ1	protein	220	72% helix, 0% strand	O13852
B, H	Protection of telomeres protein TPZ1	protein	29	72% helix, 0% strand	O14246
C, L	DNA-binding protein RAP1	protein	17	0% helix, 0% strand	Q96TL7
D	Protection of telomeres protein POZ1	protein	216	74% helix, 0% strand	O13852
E, K	Protection of telomeres protein TPZ1	protein	29	72% helix, 0% strand	O14246
F	DNA-binding protein RAP1	protein	19	0% helix, 0% strand	Q96TL7
G	Protection of telomeres protein POZ1	protein	218	73% helix, 0% strand	O13852
I	DNA-binding protein RAP1	protein	16	0% helix, 0% strand	Q96TL7
J	Protection of telomeres protein POZ1	protein	218	74% helix, 0% strand	O13852

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B, D, E, G, H, J, K

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	576	0.66	0.76	54	empty
2	379	0.62	0.77	36	empty
3	162	0.60	0.83	21	empty
4	131	0.57	0.83	22	empty
5	117	0.39	0.75	16	empty

Interfaces

12 interfaces between chains.

D–E · 1304 Å² buried · 18 hydrogen bonds · protein-protein
G–H · 1287 Å² buried · 16 hydrogen bonds · protein-protein
J–K · 1274 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 1235 Å² buried · 13 hydrogen bonds · protein-protein
D–F · 1052 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

5WE0 · Structural Basis for Shelterin Bridge Assembly · the same entry in another collection · chain L against L, 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 O13852
Every structure of UniProt O14246
Every structure of UniProt Q96TL7
Elsewhere: RCSB PDB 5WE0 · PDBe 5WE0 · UniProt O13852 · UniProt O14246 · UniProt Q96TL7

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