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1.9 ångström crystal structure of CLEC5A

Analyse 1.9 ångström crystal structure of CLEC5A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YHF
Type
protein
Length
1,062 residues
Chains
9
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
C-type lectin domain family 5 member a
UniProt
Q9NY25
Pockets
10 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, IC-type lectin domain family 5 member aprotein11817% helix, 36% strandQ9NY25

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111650.790.81115empty
211590.760.79118empty
3880.620.9024empty
41690.590.8328empty
52280.570.7924empty

Interfaces

17 interfaces between chains.

  • A–F · 872 Ų buried · 12 hydrogen bonds · protein-protein
  • B–D · 864 Ų buried · 18 hydrogen bonds · protein-protein
  • E–F · 576 Ų buried · 8 hydrogen bonds · protein-protein
  • A–B · 556 Ų buried · 8 hydrogen bonds · protein-protein
  • A–C · 555 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 27 disulfide (disulfide).

Compared structures

  • 2YHF · 1.9 Angstrom Crystal Structure of CLEC5A · the same entry in another collection · chain I against I, TM-score 1.00
  • Q9NY25 · AlphaFold monomer V2.0 prediction for C-type lectin domain family 5 member a (Q9NY25) · a predicted model of the same protein · chain F against A, TM-score 0.99

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