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The structure of a sensor domain of a histidine kinase from vibrio cholerae O1 biovar eltor str. N16961

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PDB: 4R7Q
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sensor histidine kinase
UniProt: Q9KM24
Ligands: SO4
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sensor histidine kinase	protein	213	47% helix, 12% strand	Q9KM24

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A
GOL · Glycerol · additive · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	130	0.42	0.75	22	empty

Modifications

Observed in the structure: 4 modified, 2 disulfide (engineered, disulfide).

Compared structures

4R7Q · The structure of a sensor domain of a histidine kinase from Vibrio cholerae O1 biovar… · 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 Q9KM24
Elsewhere: RCSB PDB 4R7Q · PDBe 4R7Q · UniProt Q9KM24

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