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Crystal structure of putative phosphatase from streptococcus mutans UA159

Analyse Crystal structure of putative phosphatase from streptococcus mutans UA159 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WVI
Type
protein
Length
1,012 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative phosphatases involved in N-acetyl-glucosamine catabolism
UniProt
Q8DTD6
Pockets
8 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DPutative phosphatases involved in N-acetyl-glucosamine catabolismprotein25341% helix, 23% strandQ8DTD6

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16950.770.8282empty
28960.770.8083empty
33570.680.8141empty
42730.670.8338empty
52180.560.7929empty

Interfaces

4 interfaces between chains.

  • B–C · 1198 Ų buried · 18 hydrogen bonds · protein-protein
  • A–D · 1170 Ų buried · 13 hydrogen bonds · protein-protein
  • B–D · 1067 Ų buried · 18 hydrogen bonds · protein-protein
  • A–C · 1011 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 1WVI · Crystal structure of putative phosphatase from Streptococcus mutans UA159 · the same entry in another collection · chain A against A, TM-score 1.00

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