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Structure of dipeptidyl-peptidase III from Corallococcus sp. strain EGB

Analyse Structure of dipeptidyl-peptidase III from Corallococcus sp. strain EGB in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ZUM
Type
protein
Length
1,070 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.9
Source
Corallococcus sp. EGB
Molecule
dipeptidyl-peptidase III
Ligands
ZN
Pockets
15 · best druggability 0.85

Structure

x-ray diffraction · resolution 1.9 · 2 distinct chains · 55% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
Adipeptidyl-peptidase IIIprotein53355% helix, 14% strand—
Bdipeptidyl-peptidase IIIprotein53756% helix, 14% strand—

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

15 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13210.850.9554ZN
27530.840.88100empty
32300.830.9638empty
46810.800.8479empty
52820.720.8628empty

Interfaces

1 interface between chains.

  • A–B · 1450 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified (engineered).

Compared structures

  • 5ZUM · Structure of dipeptidyl-peptidase III from corallococcus sp. strain egb · the same entry in another collection · chain A against A, TM-score 1.00

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