Research workbench
Crystal structure of pseudomonas putida methionine gamma-lyase Q349S mutant with L-methionine intermediates
Analyse Crystal structure of pseudomonas putida methionine gamma-lyase Q349S mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F1U
- Type
- protein
- Length
- 1,572 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-methionine gamma-lyase
- EC
- 4.4.1.11, 4.4.1.2
- UniProt
- P13254
- Ligands
- 3LM, MET
- Pockets
- 10 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-methionine gamma-lyase (EC 4.4.1.11, 4.4.1.2) | protein | 396 | 41% helix, 16% strand | P13254 |
| B, C, D | L-methionine gamma-lyase (EC 4.4.1.11, 4.4.1.2) | protein | 392 | 42% helix, 17% strand | P13254 |
Ligands and binding sites
- 3LM · (2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-4-(methylsulfanyl)but-2-enoic acid · ligand · 3 copies · chains A, B, C, D
- MET · Methionine · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 350 | 0.79 | 0.89 | 65 | empty |
| 2 | 275 | 0.79 | 0.90 | 48 | empty |
| 3 | 335 | 0.71 | 0.84 | 64 | 3LM |
| 4 | 296 | 0.69 | 0.83 | 58 | 3LM |
| 5 | 427 | 0.68 | 0.80 | 61 | MET |
Interfaces
6 interfaces between chains.
- A–B · 2675 Ų buried · 43 hydrogen bonds · protein-protein
- C–D · 2664 Ų buried · 39 hydrogen bonds · protein-protein
- B–C · 1605 Ų buried · 24 hydrogen bonds · protein-protein
- A–D · 1570 Ų buried · 22 hydrogen bonds · protein-protein
- B–D · 765 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, cofactor).
Compared structures
- 7F1U · Crystal structure of Pseudomonas putida methionine gamma-lyase Q349S mutant with… · the same entry in another collection · chain D against D, TM-score 1.00
- P13254 · AlphaFold monomer V2.0 prediction for L-methionine gamma-lyase (P13254) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P13254
- Elsewhere: RCSB PDB 7F1U · PDBe 7F1U · UniProt P13254
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