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Crystal structure of catalytic domain of protein O-mannosyl kinase in ligand-free form

Analyse Crystal structure of catalytic domain of protein O-mannosyl kinase in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5GZ8
Type
protein
Length
272 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein O-mannose kinase
EC
2.7.1.-
UniProt
Q3TUA9
Pockets
2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein O-mannose kinase (EC 2.7.1.-)protein27239% helix, 19% strandQ3TUA9

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13350.630.7938empty
2590.270.7315empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 5GZ8 · Crystal structure of catalytic domain of Protein O-mannosyl Kinase in ligand-free form · the same entry in another collection · chain A against A, TM-score 1.00
  • Q3TUA9 · AlphaFold monomer V2.0 prediction for protein O-mannose kinase (Q3TUA9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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