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Closed dimer of human ATM (Ataxia telangiectasia mutated)

Analyse Closed dimer of human ATM (Ataxia telangiectasia mutated) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NP0
Type: protein
Length: 5,056 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 5.7
Source: Homo sapiens
Molecule: Serine-protein kinase ATM
EC: 2.7.11.1
UniProt: Q13315
Pockets: 20 · best druggability 0.82

Structure

electron microscopy · resolution 5.7 · 1 distinct chain · 65% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Serine-protein kinase ATM (EC 2.7.11.1)	protein	2528	65% helix, 1% strand	Q13315

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	1150	0.82	0.83	145	empty
2	1110	0.82	0.83	154	empty
3	1171	0.82	0.83	150	empty
4	1142	0.81	0.82	143	empty
5	725	0.79	0.83	94	empty

Interfaces

1 interface between chains.

A–B · 547 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5NP0 · Closed dimer of human atm (ataxia telangiectasia mutated) · the same entry in another collection · chain A against A, 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 Q13315
Elsewhere: RCSB PDB 5NP0 · PDBe 5NP0 · UniProt Q13315

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