Research workbench
Crystal structure of the meth reactivation domain bound to sinefungin
Analyse Crystal structure of the meth reactivation domain bound to sinefungin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BDY
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine synthase
- EC
- 2.1.1.13
- UniProt
- P13009
- Ligands
- SFG
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine synthase (EC 2.1.1.13) | protein | 326 | 41% helix, 18% strand | P13009 |
Ligands and binding sites
- SFG · Sinefungin · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 188 | 0.52 | 0.78 | 32 | SFG |
Compared structures
- 6BDY · Crystal Structure of the MetH Reactivation Domain bound to Sinefungin · the same entry in another collection · chain A against A, TM-score 1.00
- P13009 · AlphaFold monomer V2.0 prediction for methionine synthase (P13009) · a predicted model of the same protein · chain A 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 P13009
- Elsewhere: RCSB PDB 6BDY · PDBe 6BDY · UniProt P13009
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