1.3A structure of alpha-lytic protease bound to ac-alaalapro-alanal

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 55% strand (DSSP).

Ligands and binding sites

• ACE · Acetyl group · ligand · 2 copies · chains A, B, C, D
• 2A1 · (2S)-2-aminopropan-1-ol · ligand · 2 copies · chains A, B, C, D
• SO4 · Sulfate ion · ion · 7 copies · chains A, C
• EDO · 1,2-ethanediol · additive · 5 copies · chains A, C, D
• TFA · trifluoroacetic acid · additive · 4 copies · chains A, C

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

Pockets

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

Interfaces

3 interfaces between chains.

• A–B · 279 Ų buried · 4 hydrogen bonds · protein-protein
• C–D · 263 Ų buried · 3 hydrogen bonds · protein-protein
• A–C · 118 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 covalent, 2 disulfide (covalent ligand, disulfide).

Compared structures

• 3QGJ · 1.3A Structure of alpha-Lytic Protease Bound to Ac-AlaAlaPro-Alanal · the same entry in another collection · chain A against A, TM-score 1.00
• P00778 · AlphaFold monomer V2.0 prediction for alpha-lytic protease (P00778) · a predicted model of the same protein · 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 P00778
• Elsewhere: RCSB PDB 3QGJ · PDBe 3QGJ · UniProt P00778