Research workbench
Crystal structure of L-methionine-lyase from pseudomonas
Analyse Crystal structure of L-methionine-lyase from pseudomonas in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O7C
- 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
- 9 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Methionine gamma-lyase (EC 4.4.1.11) | protein | 398 | 42% helix, 17% strand | P13254 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 651 | 0.86 | 0.90 | 93 | empty |
| 2 | 487 | 0.75 | 0.83 | 38 | SO4 |
| 3 | 577 | 0.74 | 0.81 | 54 | SO4 |
| 4 | 519 | 0.73 | 0.81 | 41 | SO4 |
| 5 | 584 | 0.72 | 0.79 | 49 | SO4 |
Interfaces
6 interfaces between chains.
- A–B · 2602 Ų buried · 44 hydrogen bonds · protein-protein
- C–D · 2581 Ų buried · 46 hydrogen bonds · protein-protein
- A–C · 1820 Ų buried · 21 hydrogen bonds · protein-protein
- B–D · 1769 Ų buried · 28 hydrogen bonds · protein-protein
- A–D · 744 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (cofactor).
Compared structures
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 2O7C · PDBe 2O7C · UniProt P13254
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