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1.9 ångström resolution crystal structure of a plant cysteine protease ervatamin-C refinement with cdna derived amino acid sequence

Analyse 1.9 ångström resolution crystal structure of a plant cysteine protease… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2PNS
Type
protein
Length
416 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ervatamin-C, a papain-like plant cysteine protease
EC
3.4.22.-
UniProt
P83654
Ligands
THJ, PO4
Pockets
3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BErvatamin-C, a papain-like plant cysteine protease (EC 3.4.22.-)protein20827% helix, 21% strandP83654

Ligands and binding sites

  • THJ · Thiosulfate · ligand · 2 copies · chains A, B
  • PO4 · Phosphate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16920.730.7962empty
21090.510.8125empty
3520.290.7515empty

Interfaces

1 interface between chains.

  • A–B · 606 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide, 2 covalent (disulfide, covalent ligand).

Compared structures

  • 2PNS · 1.9 Angstrom resolution crystal structure of a plant cysteine protease Ervatamin-C… · the same entry in another collection · chain A against A, TM-score 1.00

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