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Crystal structure of prolyl tripeptidyl aminopeptidase from porphyromonas gingivalis

Analyse Crystal structure of prolyl tripeptidyl aminopeptidase from porphyromonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2D5L
Type
protein
Length
665 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dipeptidyl aminopeptidase IV, putative
EC
3.4.14.-
UniProt
Q7MUW6
Ligands
SO4
Pockets
5 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADipeptidyl aminopeptidase IV, putative (EC 3.4.14.-)protein66515% helix, 37% strandQ7MUW6

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17960.780.8190empty
21930.520.7826empty
32720.510.7446empty
4680.360.7718empty
5670.350.7620empty

Compared structures

  • 2D5L · Crystal Structure of Prolyl Tripeptidyl Aminopeptidase from Porphyromonas gingivalis · the same entry in another collection · chain A against A, TM-score 1.00
  • Q7MUW6 · AlphaFold monomer V2.0 prediction for prolyl tripeptidyl peptidase (Q7MUW6) · a predicted model of the same protein · chain A against A, TM-score 0.99

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