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Modulating the function of human serine racemase and human serine dehydratase by protein engineering

Analyse Modulating the function of human serine racemase and human serine dehydratase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4H27
Type
protein
Length
318 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-serine DEHYDRATASE/L-threonine deaminase
EC
4.3.1.17, 4.3.1.19
UniProt
P20132
Ligands
SO4
Pockets
1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AL-serine DEHYDRATASE/L-threonine deaminase (EC 4.3.1.17, 4.3.1.19)protein31846% helix, 17% strandP20132

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14750.640.7749SO4

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

  • 4H27 · Modulating the function of human serine racemase and human serine dehydratase by protein… · the same entry in another collection · chain A against A, TM-score 1.00
  • P20132 · AlphaFold monomer V2.0 prediction for L-serine DEHYDRATASE/L-threonine deaminase (P20132) · a predicted model of the same protein · chain A against A, TM-score 0.99

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