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Metal exchange in thermolysin

Analyse Metal exchange in thermolysin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3FB0
Type
protein
Length
316 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Thermolysin
EC
3.4.24.27
UniProt
P00800
Ligands
CA
Pockets
1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AThermolysin (EC 3.4.24.27)protein31642% helix, 17% strandP00800

Ligands and binding sites

  • CA · Calcium ion · metal · 4 copies · chains A
  • DMS · Dimethyl sulfoxide · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11020.450.7922empty

Compared structures

  • 3FB0 · Metal exchange in thermolysin · the same entry in another collection · chain A against A, TM-score 1.00

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