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Crystal structure of selenomonas ruminantium phytase

Analyse Crystal structure of selenomonas ruminantium phytase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1U24
Type
protein
Length
628 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Myo-inositol hexaphosphate phosphohydrolase
EC
3.1.3.72
UniProt
Q7WUJ1
Pockets
5 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMyo-inositol hexaphosphate phosphohydrolase (EC 3.1.3.72)protein31438% helix, 17% strandQ7WUJ1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13070.580.7737empty
23190.570.7645empty
31890.530.7833empty
41460.490.7823empty
51270.480.7918empty

Interfaces

1 interface between chains.

  • A–B · 245 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 1U24 · Crystal structure of Selenomonas ruminantium phytase · the same entry in another collection · chain A against A, TM-score 1.00

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