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ATPase

Analyse ATPase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6J18
Type: protein
Length: 272 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2
Source: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Molecule: ESX-5 secretion system protein EccC5
UniProt: P9WNA5
Ligands: ATP, MG
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · resolution 2 · 1 distinct chain · 26% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ESX-5 secretion system protein EccC5	protein	272	26% helix, 23% strand	P9WNA5

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	199	0.52	0.77	29	empty
2	116	0.50	0.81	25	ATP, MG
3	66	0.38	0.78	12	empty

Compared structures

6J18 · ATPASE · the same entry in another collection · chain A against A, TM-score 1.00
P9WNA5 · AlphaFold monomer V2.0 prediction for esx-5 secretion system protein ECCC5 (P9WNA5) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P9WNA5
Elsewhere: RCSB PDB 6J18 · PDBe 6J18 · UniProt P9WNA5

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