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Aspartic proteinase SAPP2 secreted from candida parapsilosis at 0.82 a resolution.

Analyse Aspartic proteinase SAPP2 secreted from candida parapsilosis at 0.82 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4Y9W
Type
protein
Length
332 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Aspartic acid endopeptidase SAPP2; Peptide
UniProt
G8B6Y8
Ligands
IVA
Pockets
1 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAspartic acid endopeptidase SAPP2protein32712% helix, 50% strandG8B6Y8
BPeptideprotein50% helix, 40% strand—

Ligands and binding sites

  • IVA · Isovaleric acid · ligand · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11550.410.7328IVA

Interfaces

1 interface between chains.

  • A–B · 610 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 4Y9W · Aspartic Proteinase Sapp2 Secreted from Candida Parapsilosis at 0.82 A Resolution. · the same entry in another collection · chain A against A, TM-score 1.00

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