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Automated refinement of diffraction data obtained from an endothiapepsin crystal treated with fragment 262

Analyse Automated refinement of diffraction data obtained from an endothiapepsin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5P61
Type
protein
Length
330 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Endothiapepsin
EC
3.4.23.22
UniProt
P11838
Pockets
1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndothiapepsin (EC 3.4.23.22)protein33011% helix, 45% strandP11838

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13060.580.7638empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 5P61 · Automated refinement of diffraction data obtained from an endothiapepsin crystal treated… · 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

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