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Major aspartyl peptidase 1 from C. neoformans

Analyse Major aspartyl peptidase 1 from C. neoformans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6R5H
Type
protein
Length
350 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Endopeptidase
UniProt
J9VS02
Ligands
NAG, NA, SO4
Pockets
1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndopeptidaseprotein35011% helix, 44% strandJ9VS02

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
  • NA · Sodium ion · metal · 2 copies · chains A
  • SO4 · Sulfate ion · ion · 4 copies · chains A
  • PEG · Di(hydroxyethyl)ether · additive · 7 copies · chains A
  • PGE · Triethylene glycol · additive · chains A
  • EDO · 1,2-ethanediol · additive · chains A
  • ACY · Acetic acid · additive · chains A
  • PG4 · Tetraethylene glycol · additive · chains A
  • 1PE · Pentaethylene glycol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13370.590.7645PEG, NA

Modifications

Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • 6R5H · Major aspartyl peptidase 1 from C. neoformans · the same entry in another collection · chain A against A, TM-score 1.00

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