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The crystal structure of the gaf domain of a two-component sensor histidine kinase from bacillus halodurans to 2.45A

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

PDB
3O5Y
Type
protein
Length
289 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sensor protein
EC
2.7.13.3
UniProt
Q9KFE5
Pockets
2 · best druggability 0.39

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASensor protein (EC 2.7.13.3)protein14233% helix, 27% strandQ9KFE5
BSensor protein (EC 2.7.13.3)protein14734% helix, 25% strandQ9KFE5

Ligands and binding sites

  • ACT · Acetate ion · additive · 3 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1620.390.8014empty
2620.300.7520empty

Interfaces

1 interface between chains.

  • A–B · 452 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 3O5Y · The Crystal Structure of the GAF domain of a two-component sensor histidine kinase from… · the same entry in another collection · chain A against A, TM-score 1.00

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