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Crystal structure of human pro-granzyme K

Analyse Crystal structure of human pro-granzyme K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1MZD
Type
protein
Length
240 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pro-granzyme K
EC
3.4.21.-
UniProt
P49863
Pockets
3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APro-granzyme K (EC 3.4.21.-)protein2406% helix, 31% strandP49863

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11900.510.7731empty
21440.440.7630empty
3630.400.8125empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 1MZD · crystal structure of human pro-granzyme K · the same entry in another collection · chain A against A, TM-score 1.00
  • P49863 · AlphaFold monomer V2.0 prediction for granzyme K (P49863) · a predicted model of the same protein · chain A against A, TM-score 0.93

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