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Crystal structure of human cln protein 5 (ceroid lipofuscinosis neuronal protein 5)

Analyse Crystal structure of human cln protein 5 (ceroid lipofuscinosis neuronal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6R99
Type
protein
Length
285 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ceroid-lipofuscinosis neuronal protein 5
UniProt
A0A024R644
Ligands
NAG, BMA
Pockets
4 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACeroid-lipofuscinosis neuronal protein 5protein28526% helix, 33% strandA0A024R644

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
  • BMA · beta-D-mannopyranose · sugar · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12490.560.7847empty
2880.420.7819empty
3630.280.7314empty
4690.280.7212empty

Modifications

Observed in the structure: 7 modified, 4 glycan, 2 disulfide (engineered, N-glycosylation, disulfide).

Compared structures

  • 6R99 · Crystal Structure of Human CLN protein 5 (Ceroid Lipofuscinosis Neuronal Protein 5) · the same entry in another collection · chain A against A, TM-score 1.00

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