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The active site of aspartic proteinases

Analyse The active site of aspartic proteinases in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4APE
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.1
Source: Cryphonectria parasitica
Molecule: Endothiapepsin
EC: 3.4.23.10
UniProt: P11838
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · resolution 2.1 · 1 distinct chain · 9% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endothiapepsin (EC 3.4.23.10)	protein	330	9% helix, 47% strand	P11838

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	310	0.59	0.77	36	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4APE · The active site of aspartic proteinases · the same entry in another collection · chain A against A, TM-score 1.00
P11838 · AlphaFold monomer V2.0 prediction for endothiapepsin (P11838) · 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 P11838
Elsewhere: RCSB PDB 4APE · PDBe 4APE · UniProt P11838

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