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Structure of the D223N mutant of selenomonas ruminantium ptp-like phytase

Analyse Structure of the D223N mutant of selenomonas ruminantium ptp-like phytase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2B4P
Type
protein
Length
627 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
Ligands
CL
Pockets
5 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMyo-inositol hexaphosphate phosphohydrolase (EC 3.1.3.72)protein31439% helix, 18% strandQ7WUJ1
BMyo-inositol hexaphosphate phosphohydrolase (EC 3.1.3.72)protein31340% helix, 18% strandQ7WUJ1

Ligands and binding sites

  • CL · Chloride ion · ion · 2 copies · chains B
  • MLI · Malonate ion · additive · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13630.610.7730empty
23200.580.7748MLI
32760.570.7744MLI
41410.520.8032empty
51110.490.8125CL

Interfaces

1 interface between chains.

  • A–B · 711 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 2B4P · Structure of the D223N mutant of Selenomonas ruminantium PTP-like phytase · the same entry in another collection · chain A against A, TM-score 1.00

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