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L-methionine gamma-lyase from citrobacter freundii with Y58F substitution

Analyse L-methionine gamma-lyase from citrobacter freundii with Y58F substitution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4P7Y
Type
protein
Length
396 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methionine gamma-lyase
UniProt
M3DJ89
Pockets
3 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMethionine gamma-lyaseprotein39642% helix, 16% strandM3DJ89

Ligands and binding sites

  • PEG · Di(hydroxyethyl)ether · additive · chains A
  • 1PE · Pentaethylene glycol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12330.530.7730empty
21650.500.7829empty
3720.330.7516empty

Modifications

Observed in the structure: 2 modified (cofactor, oxidation).

Compared structures

  • 4P7Y · L-methionine gamma-lyase from Citrobacter freundii with Y58F substitution · the same entry in another collection · chain A against A, TM-score 1.00

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