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Crystal structure of a pas domain from two-component sensor histidine kinase

Analyse Crystal structure of a pas domain from two-component sensor histidine kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OLO
Type
protein
Length
221 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Two-component sensor histidine kinase
EC
2.7.13.3
UniProt
Q8YZM9
Pockets
1 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATwo-component sensor histidine kinase (EC 2.7.13.3)protein11134% helix, 40% strandQ8YZM9
BTwo-component sensor histidine kinase (EC 2.7.13.3)protein11031% helix, 41% strandQ8YZM9

Ligands and binding sites

  • GOL · Glycerol · additive · 2 copies · chains A, B

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1530.310.7712empty

Interfaces

1 interface between chains.

  • A–B · 25 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 3OLO · Crystal structure of a PAS domain from two-component sensor histidine kinase · the same entry in another collection · chain A against A, TM-score 1.00

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