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PanDDA analysis group deposition -- Endothiapepsin ground state model 31

Analyse PanDDA analysis group deposition -- Endothiapepsin ground state model 31 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5RD9
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.11
Source: Cryphonectria parasitica
Molecule: Endothiapepsin
EC: 3.4.23.22
UniProt: P11838
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · resolution 1.11 · 1 distinct chain · 10% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endothiapepsin (EC 3.4.23.22)	protein	330	10% helix, 45% 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	331	0.58	0.76	39	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5RD9 · Pandda analysis group deposition -- endothiapepsin ground state model 31 · 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 5RD9 · PDBe 5RD9 · UniProt P11838

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