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Crystal structure of CBLN4

Analyse Crystal structure of CBLN4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5H4C
Type
protein
Length
401 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein CBLN4
UniProt
D4ABJ2
Ligands
NAG
Pockets
3 · best druggability 0.83

Structure

x-ray diffraction · 3 distinct chains · 2% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein CBLN4protein1344% helix, 51% strandD4ABJ2
BProtein CBLN4protein1353% helix, 54% strandD4ABJ2
CProtein CBLN4protein1320% helix, 54% strandD4ABJ2

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12040.830.9742empty
21840.760.9241empty
31740.520.7821empty

Interfaces

3 interfaces between chains.

  • A–C · 851 Ų buried · 4 hydrogen bonds · protein-protein
  • A–B · 843 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 842 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 glycan (N-glycosylation).

Compared structures

  • 5H4C · Crystal structure of Cbln4 · the same entry in another collection · chain A against A, TM-score 1.00

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