MolNFT v1 · #50354 · protein
High resolution structure of L-methionine gamma-lyase from citrobacter freundii
2RFV: “High resolution structure of L-methionine gamma-lyase from citrobacter freundii”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.54). MolNFT v1 #50354 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2RFV
- Type
- protein
- Length
- 391 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
- CL
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine gamma-lyase (EC 4.4.1.11) | protein | 391 | 42% helix, 16% strand | Q84AR1 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.54 | 0.77 | 29 | empty |
| 2 | 121 | 0.47 | 0.79 | 32 | empty |
Modifications
Observed in the structure: 2 modified (cofactor, oxidation).
Compared structures
- 2RFV · High resolution structure of L-methionine gamma-lyase from Citrobacter freundii · 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 2RFV · PDBe 2RFV · UniProt Q84AR1
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