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Crystal structure of N392L mutant of yeast bleomycin hydrolase

Analyse Crystal structure of N392L mutant of yeast bleomycin hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2E00
Type
protein
Length
457 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cysteine proteinase 1
EC
3.4.22.40
UniProt
Q01532
Pockets
5 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACysteine proteinase 1 (EC 3.4.22.40)protein45743% helix, 18% strandQ01532

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11830.660.8631empty
21240.480.7922empty
3510.430.8317empty
41320.430.7520empty
5500.270.7414empty

Compared structures

  • 2E00 · Crystal structure of N392L mutant of yeast bleomycin hydrolase · the same entry in another collection · chain A against A, TM-score 1.00
  • Q01532 · AlphaFold monomer V2.0 prediction for cysteine proteinase 1, mitochondrial (Q01532) · a predicted model of the same protein · chain A against A, TM-score 1.00

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