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Crystal structure of uricase from Arthrobacter globiformis

Analyse Crystal structure of uricase from Arthrobacter globiformis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YZE
Type
protein
Length
2,296 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.99
Source
Arthrobacter globiformis
Molecule
Uricase
EC
1.7.3.3
Ligands
NOB
Pockets
20 · best druggability 0.80

Structure

x-ray diffraction · resolution 1.99 · 1 distinct chain · 25% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, HUricase (EC 1.7.3.3)protein28725% helix, 42% strand—

Ligands and binding sites

  • NOB · (dihydroxyboranyloxy-hydroxy-boranyl)oxylithium · ligand · 8 copies · chains A, D, B, C, E, H, F, G

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110040.800.81100NOB
29710.790.8198NOB
38920.770.7983NOB
48520.760.7983NOB
59860.710.7694empty

Interfaces

15 interfaces between chains.

  • F–G · 3304 Ų buried · 56 hydrogen bonds · protein-protein
  • B–C · 3302 Ų buried · 56 hydrogen bonds · protein-protein
  • E–H · 3263 Ų buried · 55 hydrogen bonds · protein-protein
  • A–D · 3262 Ų buried · 56 hydrogen bonds · protein-protein
  • G–H · 2465 Ų buried · 51 hydrogen bonds · protein-protein

Compared structures

  • 2YZE · Crystal structure of uricase from arthrobacter globiformis · the same entry in another collection · chain A against A, TM-score 1.00

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