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The crystal structure of L-threonine-O-3-phosphate decarboxylase from porphyromonas gingivalis

Analyse The crystal structure of L-threonine-O-3-phosphate decarboxylase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3FKD
Type
protein
Length
1,286 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-threonine-O-3-phosphate decarboxylase
UniProt
Q7MXY2
Pockets
18 · best druggability 0.79

Structure

x-ray diffraction · 4 distinct chains · 41% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AL-threonine-O-3-phosphate decarboxylaseprotein32641% helix, 17% strandQ7MXY2
BL-threonine-O-3-phosphate decarboxylaseprotein32542% helix, 17% strandQ7MXY2
CL-threonine-O-3-phosphate decarboxylaseprotein32542% helix, 18% strandQ7MXY2
DL-threonine-O-3-phosphate decarboxylaseprotein31040% helix, 17% strandQ7MXY2

Pockets

18 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14150.790.8859empty
23910.790.8854empty
34270.720.8252empty
43300.640.8047empty
53310.620.7929empty

Interfaces

5 interfaces between chains.

  • B–C · 1684 Ų buried · 26 hydrogen bonds · protein-protein
  • A–D · 1671 Ų buried · 22 hydrogen bonds · protein-protein
  • B–D · 614 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 367 Ų buried · 0 hydrogen bonds · protein-protein
  • A–B · 110 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 27 modified (engineered).

Compared structures

  • 3FKD · The crystal structure of L-threonine-O-3-phosphate decarboxylase from Porphyromonas… · the same entry in another collection · chain A against A, TM-score 1.00

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