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Structural and catalytic analysis of two diverse uridine phosphorylases in the oomycete phytophthora capsici.

Analyse Structural and catalytic analysis of two diverse uridine phosphorylases in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6KD3
Type
protein
Length
588 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uridine phosphorylase
EC
2.4.2.3
Pockets
5 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BUridine phosphorylase (EC 2.4.2.3)protein29430% helix, 17% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18990.830.85127empty
24300.720.8345empty
34220.710.8239empty
4650.360.7718empty
5510.350.7913empty

Interfaces

1 interface between chains.

  • A–B · 2397 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

  • 6KD3 · Structural and catalytic analysis of two diverse uridine phosphorylases in the oomycete… · the same entry in another collection · chain A against A, TM-score 1.00

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