MolNFT v1 · #68452 · protein

Crystal structure of L-methionine gamma-lyase from citrobacter freundii with methionine phosphinate

3JWA: “Crystal structure of L-methionine gamma-lyase from citrobacter freundii with methionine phosphinate”. X-ray diffraction, 1 ligand (MPJ), 3 pockets (best druggability 0.56). MolNFT v1 #68452 on GenesisL1: 3D structure, binding sites…

PDB: 3JWA
Type: protein
Length: 396 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methionine gamma-lyase
EC: 4.4.1.11
UniProt: Q84AR1
Ligands: MPJ
Pockets: 3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methionine gamma-lyase (EC 4.4.1.11)	protein	396	41% helix, 15% strand	Q84AR1

Ligands and binding sites

MPJ · (1-amino-3-methylsulfanyl-propyl)-phosphinic acid · ligand · chains A
PEG · Di(hydroxyethyl)ether · additive · 5 copies · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	221	0.56	0.79	35	empty
2	227	0.55	0.78	31	MPJ
3	71	0.36	0.77	15	empty

Modifications

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

Compared structures

3JWA · Crystal structure of L-methionine gamma-lyase from Citrobacter freundii with methionine… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q84AR1
Elsewhere: RCSB PDB 3JWA · PDBe 3JWA · UniProt Q84AR1

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