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Intracellular subtilisin precursor from B. clausii

Analyse Intracellular subtilisin precursor from B. clausii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2WV7
Type
protein
Length
1,785 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Intracellular subtilisin protease
EC
3.4.21.62
UniProt
D0AB41
Ligands
NA
Pockets
12 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, EIntracellular subtilisin protease (EC 3.4.21.62)protein29830% helix, 24% strandD0AB41
FIntracellular subtilisin protease (EC 3.4.21.62)protein29531% helix, 23% strandD0AB41

Ligands and binding sites

  • NA · Sodium ion · metal · 5 copies · chains B, C, D, E, F

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

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12280.580.7928empty
22120.550.7828empty
32270.540.7728empty
41810.520.7827empty
51690.510.7826empty

Interfaces

5 interfaces between chains.

  • E–F · 1601 Ų buried · 21 hydrogen bonds · protein-protein
  • C–D · 1601 Ų buried · 22 hydrogen bonds · protein-protein
  • A–B · 1584 Ų buried · 20 hydrogen bonds · protein-protein
  • B–E · 447 Ų buried · 8 hydrogen bonds · protein-protein
  • A–C · 250 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 2WV7 · Intracellular subtilisin precursor from B. clausii · the same entry in another collection · chain A against A, TM-score 1.00

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