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N-terminal domain of human conserved dopamine neurotrophic factor (cdnf)

Analyse N-terminal domain of human conserved dopamine neurotrophic factor (cdnf) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2W50
Type
protein
Length
194 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Armet-like protein 1
UniProt
Q49AH0
Ligands
PO4
Pockets
2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BArmet-like protein 1protein9763% helix, 0% strandQ49AH0

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 4 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12420.530.7638empty
2750.340.7518empty

Interfaces

1 interface between chains.

  • A–B · 429 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 2W50 · N-terminal domain of human conserved dopamine neurotrophic factor (CDNF) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q49AH0 · AlphaFold monomer V2.0 prediction for cerebral dopamine neurotrophic factor (Q49AH0) · a predicted model of the same protein · chain A against A, TM-score 0.96

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