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Structural basis of aimp signaling molecule recognition by aimr in spbeta group of bacteriophages

Analyse Structural basis of aimp signaling molecule recognition by aimr in spbeta group… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6IM4
Type
protein
Length
792 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Aimr transcriptional regulator; Gly-met-pro-arg-gly-ala
UniProt
O64094
Pockets
9 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 70% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAimr transcriptional regulatorprotein39072% helix, 0% strandO64094
C, DGly-met-pro-arg-gly-alaprotein60% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15580.670.7755empty
24260.660.7941empty
34070.640.7840empty
41530.430.7524empty
5890.380.7614empty

Interfaces

3 interfaces between chains.

  • A–D · 571 Ų buried · 12 hydrogen bonds · protein-protein
  • B–C · 567 Ų buried · 11 hydrogen bonds · protein-protein
  • A–B · 245 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 6IM4 · Structural basis of AimP signaling molecule recognition by AimR in Spbeta group of… · the same entry in another collection · chain A against A, TM-score 1.00

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