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PanDDA analysis group deposition -- Auto-refined data of Endothiapepsin for ground state model 51, DMSO-Free

Analyse PanDDA analysis group deposition -- Auto-refined data of Endothiapepsin for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5R3R
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 0.979
Source: Cryphonectria parasitica
Molecule: Endothiapepsin
EC: 3.4.23.22
UniProt: P11838
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · resolution 0.979 · 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	281	0.56	0.77	31	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5R3R · Pandda analysis group deposition -- auto-refined data of endothiapepsin for ground state… · 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 5R3R · PDBe 5R3R · UniProt P11838

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