Major aspartyl peptidase 1 from C. neoformans

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 44% strand (DSSP).

Ligands and binding sites

• IVA · Isovaleric acid · ligand · chains A, D
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
• NA · Sodium ion · metal · chains A
• SO4 · Sulfate ion · ion · 6 copies · chains A
• PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
• 1PE · Pentaethylene glycol · additive · 2 copies · chains A
• PGE · Triethylene glycol · additive · chains A

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

Interfaces

1 interface between chains.

• A–D · 584 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

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

Compared structures

• 6R6A · Major aspartyl peptidase 1 from C. neoformans · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt J9VS02
• Elsewhere: RCSB PDB 6R6A · PDBe 6R6A · UniProt J9VS02