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Detailed structure of L-methionine-lyase from pseudomonas putida

Analyse Detailed structure of L-methionine-lyase from pseudomonas putida in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1UKJ
Type
protein
Length
1,592 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Methionine gamma-lyase
EC
4.4.1.11
UniProt
P13254
Ligands
SO4
Pockets
10 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DMethionine gamma-lyase (EC 4.4.1.11)protein39840% helix, 17% strandP13254

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 5 copies · chains A, B, C, D

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

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17160.850.8998SO4
25110.750.8339SO4
34730.740.8341SO4
45230.730.8136SO4
55670.730.8045SO4

Interfaces

6 interfaces between chains.

  • A–B · 2597 Ų buried · 42 hydrogen bonds · protein-protein
  • C–D · 2587 Ų buried · 44 hydrogen bonds · protein-protein
  • A–C · 1794 Ų buried · 19 hydrogen bonds · protein-protein
  • B–D · 1753 Ų buried · 25 hydrogen bonds · protein-protein
  • A–D · 733 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (cofactor).

Compared structures

  • 1UKJ · Detailed structure of L-Methionine-Lyase from Pseudomonas putida · the same entry in another collection · chain A against A, TM-score 1.00
  • P13254 · AlphaFold monomer V2.0 prediction for L-methionine gamma-lyase (P13254) · a predicted model of the same protein · chain A against A, TM-score 0.99

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