Research workbench

Legionella pneumophila effector AnkD

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

PDB: 7EW8
Type: protein
Length: 860 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.594
Source: Legionella pneumophila
Molecule: ANK_REP_REGION domain-containing protein
UniProt: A0A2S6F2G5
Pockets: 17 · best druggability 0.55

Structure

x-ray diffraction · resolution 2.594 · 2 distinct chains · 55% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ANK_REP_REGION domain-containing protein	protein	431	55% helix, 9% strand	A0A2S6F2G5
B	ANK_REP_REGION domain-containing protein	protein	429	55% helix, 9% strand	A0A2S6F2G5

Pockets

17 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	191	0.55	0.79	40	empty
2	99	0.54	0.84	22	empty
3	250	0.54	0.77	30	empty
4	284	0.51	0.74	30	empty
5	205	0.50	0.76	26	empty

Interfaces

1 interface between chains.

A–B · 235 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 modified (engineered).

Compared structures

7EW8 · Legionella pneumophila effector ankd · 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 A0A2S6F2G5
Elsewhere: RCSB PDB 7EW8 · PDBe 7EW8 · UniProt A0A2S6F2G5

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