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The mutant Y218C of deinococcus radiodurans N-acylamino acid racemase

Analyse The mutant Y218C of deinococcus radiodurans N-acylamino acid racemase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2GGJ
Type
protein
Length
1,440 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-acylamino acid racemase
EC
5.1.1.10
UniProt
Q9RYA6
Pockets
7 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DN-acylamino acid racemase (EC 5.1.1.10)protein36036% helix, 23% strandQ9RYA6

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15120.780.8557empty
27130.780.8383empty
36770.730.8068empty
43550.590.7736empty
53440.580.7741empty

Interfaces

3 interfaces between chains.

  • B–D · 1254 Ų buried · 21 hydrogen bonds · protein-protein
  • A–C · 1248 Ų buried · 21 hydrogen bonds · protein-protein
  • A–B · 954 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 2GGJ · The mutant Y218C of Deinococcus Radiodurans N-acylamino acid racemase · the same entry in another collection · chain A against A, TM-score 1.00

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