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High resolution crystal structure of the intact pro-kumamolisin, a sedolisin type proteinase (previously called kumamolysin or kscp)

Analyse High resolution crystal structure of the intact pro-kumamolisin, a sedolisin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1T1E
Type
protein
Length
534 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Kumamolisin
UniProt
Q8RR56
Ligands
CA
Pockets
8 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKumamolisinprotein53428% helix, 25% strandQ8RR56

Ligands and binding sites

  • CA · Calcium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13150.590.7839empty
2930.370.7522empty
3940.360.7519empty
4810.340.7516empty
5680.340.7615empty

Compared structures

  • 1T1E · High Resolution Crystal Structure of the Intact Pro-Kumamolisin, a Sedolisin Type… · the same entry in another collection · chain A against A, TM-score 1.00

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