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Cryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex

Analyse Cryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7OLE
Type: protein
Length: 4,023 residues
Chains: 9
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.41
Source: Homo sapiens
Molecule: RuvB-like 1; RuvB-like 2; TELO2-interacting protein 1 homolog,TELO2-interacting protein 1…
EC: 3.6.4.12
UniProt: Q9Y265, Q9Y230, O43156, Q6NXR4, Q9Y4R8
Ligands: ADP
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · resolution 3.41 · 9 distinct chains · 50% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RuvB-like 1 (EC 3.6.4.12)	protein	433	25% helix, 9% strand	Q9Y265
B	RuvB-like 2 (EC 3.6.4.12)	protein	418	33% helix, 15% strand	Q9Y230
C	RuvB-like 1 (EC 3.6.4.12)	protein	427	34% helix, 17% strand	Q9Y265
D	RuvB-like 2 (EC 3.6.4.12)	protein	419	36% helix, 10% strand	Q9Y230
E	RuvB-like 1 (EC 3.6.4.12)	protein	413	38% helix, 17% strand	Q9Y265
F	RuvB-like 2 (EC 3.6.4.12)	protein	419	35% helix, 18% strand	Q9Y230
H	TELO2-interacting protein 1 homolog,TELO2-interacting protein 1 homolog,TTI1	protein	644	77% helix, 0% strand	O43156
J	TELO2-interacting protein 2,TELO2-interacting protein 2,TTI2	protein	456	80% helix, 0% strand	Q6NXR4
K	Telomere length regulation protein TEL2 homolog	protein	394	78% helix, 0% strand	Q9Y4R8

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains B, C, D, E, F

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	745	0.87	0.90	119	empty
2	1066	0.85	0.85	100	ADP
3	1131	0.83	0.84	93	ADP
4	715	0.82	0.86	120	empty
5	543	0.82	0.88	67	empty

Interfaces

11 interfaces between chains.

A–B · 2773 Å² buried · 42 hydrogen bonds · protein-protein
C–D · 1902 Å² buried · 19 hydrogen bonds · protein-protein
E–F · 1856 Å² buried · 6 hydrogen bonds · protein-protein
A–F · 1794 Å² buried · 27 hydrogen bonds · protein-protein
B–C · 1791 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 covalent (covalent ligand).

Compared structures

7OLE · Cryo-EM structure of the TELO2-TTI1-TTI2-RUVBL1-RUVBL2 complex · the same entry in another collection · chain K against K, TM-score 1.00
Q9Y4R8 · AlphaFold monomer V2.0 prediction for telomere length regulation protein TEL2 homolog… · a predicted model of the same protein · chain K against A, TM-score 0.85
O43156 · AlphaFold monomer V2.0 prediction for TELO2-interacting protein 1 homolog (O43156) · a predicted model of the same protein · chain H against A, TM-score 0.85
Q9Y230 · AlphaFold monomer V2.0 prediction for ruvb-like 2 (Q9Y230) · a predicted model of the same protein · chain F against A, TM-score 0.80

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 Q9Y265
Every structure of UniProt Q9Y230
Every structure of UniProt O43156
Every structure of UniProt Q6NXR4
Every structure of UniProt Q9Y4R8
Elsewhere: RCSB PDB 7OLE · PDBe 7OLE · UniProt Q9Y265 · UniProt Q9Y230 · UniProt O43156 · UniProt Q6NXR4 · UniProt Q9Y4R8

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