MolNFT v1 · #49333 · protein

Structural basis for activation of plant immunity by bacterial effector protein avrpto

2QKW · Avirulence protein: “Structural basis for activation of plant immunity by bacterial effector protein avrpto”. X-ray diffraction, 5 pockets (best druggability 0.75). MolNFT v1 #49333 on GenesisL1: 3D structure, binding sites and…

PDB: 2QKW
Type: protein
Length: 393 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Avirulence protein; Protein kinase
EC: 2.7.11.1
UniProt: Q08242, Q40234
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Avirulence protein	protein	101	70% helix, 3% strand	Q08242
B	Protein kinase (EC 2.7.11.1)	protein	292	34% helix, 13% strand	Q40234

Pockets

5 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	645	0.75	0.81	62	empty
2	97	0.56	0.85	19	empty
3	66	0.39	0.79	13	empty
4	114	0.38	0.74	22	empty
5	56	0.27	0.73	15	empty

Interfaces

1 interface between chains.

A–B · 755 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

2QKW · Structural basis for activation of plant immunity by bacterial effector protein AvrPto · 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 Q08242
Every structure of UniProt Q40234
Elsewhere: RCSB PDB 2QKW · PDBe 2QKW · UniProt Q08242 · UniProt Q40234

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