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Crystal structure of a propionate kinase from francisella tularensis subsp. tularensis schu S4

Analyse Crystal structure of a propionate kinase from francisella tularensis subsp.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KHY
Type: protein
Length: 768 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Propionate kinase
EC: 2.7.2.-
UniProt: Q5NE95
Pockets: 6 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Propionate kinase (EC 2.7.2.-)	protein	384	43% helix, 20% strand	Q5NE95

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	334	0.86	0.96	43	empty
2	551	0.66	0.77	60	empty
3	524	0.64	0.76	62	empty
4	81	0.43	0.80	24	empty
5	86	0.42	0.79	24	empty

Interfaces

1 interface between chains.

A–B · 2859 Å² buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 22 modified (engineered).

Compared structures

3KHY · Crystal Structure of a propionate kinase from Francisella tularensis subsp. tularensis… · 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 Q5NE95
Elsewhere: RCSB PDB 3KHY · PDBe 3KHY · UniProt Q5NE95

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