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The molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 ångströms resolution

Analyse The molecular and crystal structures of monoclinic porcine pepsin refined at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4PEP
Type
protein
Length
326 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pepsin
EC
3.4.23.1
UniProt
P00791
Pockets
2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APepsin (EC 3.4.23.1)protein32615% helix, 46% strandP00791

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12810.630.8040empty
2840.340.7517empty

Modifications

Observed in the structure: 3 disulfide, 1 modified (disulfide, phosphorylation).

Compared structures

  • 4PEP · The molecular and crystal structures of monoclinic porcine pepsin refined at 1.8… · the same entry in another collection · chain A against A, TM-score 1.00
  • P00791 · AlphaFold monomer V2.0 prediction for pepsin a (P00791) · a predicted model of the same protein · chain A against A, TM-score 0.96

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