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Crystal structure of ahrc, the arginine REPRESSOR/ACTIVATOR protein from bacillus subtilis

Analyse Crystal structure of ahrc, the arginine REPRESSOR/ACTIVATOR protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1F9N
Type
protein
Length
887 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Arginine REPRESSOR/ACTIVATOR protein
UniProt
P17893
Pockets
12 · best druggability 0.80

Structure

x-ray diffraction · 4 distinct chains · 44% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AArginine REPRESSOR/ACTIVATOR proteinprotein14745% helix, 22% strandP17893
B, FArginine REPRESSOR/ACTIVATOR proteinprotein14943% helix, 21% strandP17893
C, EArginine REPRESSOR/ACTIVATOR proteinprotein14844% helix, 21% strandP17893
DArginine REPRESSOR/ACTIVATOR proteinprotein14642% helix, 21% strandP17893

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18950.800.83121empty
24150.660.7927empty
31920.630.8433empty
42400.590.8040empty
5880.480.8221empty

Interfaces

14 interfaces between chains.

  • B–E · 1178 Ų buried · 17 hydrogen bonds · protein-protein
  • A–F · 964 Ų buried · 6 hydrogen bonds · protein-protein
  • C–D · 886 Ų buried · 6 hydrogen bonds · protein-protein
  • A–B · 466 Ų buried · 2 hydrogen bonds · protein-protein
  • D–F · 443 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 1F9N · Crystal structure of ahrc, the arginine REPRESSOR/ACTIVATOR protein from bacillus subtilis · the same entry in another collection · chain F against F, TM-score 1.00
  • P17893 · AlphaFold monomer V2.0 prediction for arginine repressor (P17893) · a predicted model of the same protein · chain D against A, TM-score 0.61

Analyse

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