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Crystal structure of human chondroadherin

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

PDB
5LFN
Type
protein
Length
1,296 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chondroadherin
UniProt
O15335
Ligands
CL
Pockets
5 · best druggability 0.82

Structure

x-ray diffraction · 3 distinct chains · 8% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BChondroadherinprotein3248% helix, 17% strandO15335
CChondroadherinprotein3238% helix, 18% strandO15335
DChondroadherinprotein3258% helix, 17% strandO15335

Ligands and binding sites

  • CL · Chloride ion · ion · 2 copies · chains B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111920.820.83113empty
29780.810.8297empty
31480.510.8024empty
41380.430.7628empty
5570.380.8015empty

Interfaces

4 interfaces between chains.

  • C–D · 1069 Ų buried · 8 hydrogen bonds · protein-protein
  • A–B · 870 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 453 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 134 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 disulfide (disulfide).

Compared structures

  • 5LFN · Crystal structure of human chondroadherin · the same entry in another collection · chain D against D, TM-score 1.00
  • O15335 · AlphaFold monomer V2.0 prediction for chondroadherin (O15335) · a predicted model of the same protein · chain C against A, TM-score 0.99

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