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The mechanisms of hamp-mediated signaling in transmembrane receptors - the A291V mutant

Analyse The mechanisms of hamp-mediated signaling in transmembrane receptors - the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Y21
Type
protein
Length
631 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hamp
UniProt
O28769
Pockets
6 · best druggability 0.69

Structure

x-ray diffraction · 9 distinct chains · 66% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, IHampprotein5267% helix, 0% strandO28769
BHampprotein5368% helix, 0% strandO28769
D, FHampprotein5569% helix, 0% strandO28769
EHampprotein5461% helix, 0% strandO28769
GHampprotein5263% helix, 0% strandO28769
HHampprotein5066% helix, 0% strandO28769
JHampprotein5469% helix, 0% strandO28769
KHampprotein4965% helix, 0% strandO28769
LHampprotein5362% helix, 0% strandO28769

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19540.690.7587empty
22960.530.7534empty
31140.370.7420empty
41030.350.7417empty
5770.340.7520empty

Interfaces

22 interfaces between chains.

  • A–B · 868 Ų buried · 13 hydrogen bonds · protein-protein
  • I–J · 860 Ų buried · 13 hydrogen bonds · protein-protein
  • E–F · 854 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 852 Ų buried · 12 hydrogen bonds · protein-protein
  • K–L · 851 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 2Y21 · The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291V mutant · the same entry in another collection · chain A against A, TM-score 1.00

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