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Crystal structure of the human adiponectin receptor 1

Analyse Crystal structure of the human adiponectin receptor 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6KS0
Type
protein
Length
512 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Adiponectin receptor protein 1; The heavy chain variable domain (antibody); The light…
UniProt
Q96A54
Ligands
ZN, PO4
Pockets
4 · best druggability 0.84

Structure

x-ray diffraction · 3 distinct chains · 41% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAdiponectin receptor protein 1protein28669% helix, 1% strandQ96A54
HThe heavy chain variable domain (antibody)protein1198% helix, 49% strand—
LThe light chain variable domain (antibody)protein1073% helix, 51% strand—

Ligands and binding sites

  • ZN · Zinc ion · metal · chains A
  • PO4 · Phosphate ion · ion · chains A, L

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15050.840.9065empty
21990.520.7740empty
3630.330.7718empty
4750.300.7425empty

Interfaces

3 interfaces between chains.

  • H–L · 820 Ų buried · 7 hydrogen bonds · protein-protein
  • A–L · 522 Ų buried · 7 hydrogen bonds · protein-protein
  • A–H · 445 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 6KS0 · Crystal structure of the human adiponectin receptor 1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96A54 · AlphaFold monomer V2.0 prediction for adiponectin receptor protein 1 (Q96A54) · a predicted model of the same protein · chain A against A, TM-score 0.97

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