Research workbench
X-ray structure of apo methanocaldococcus jannaschii methyltransferase subunit a at 1.85 ångström
Analyse X-ray structure of apo methanocaldococcus jannaschii methyltransferase subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5L8X
- Type
- protein
- Length
- 344 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetrahydromethanopterin S-methyltransferase subunit a
- EC
- 2.1.1.86
- UniProt
- Q58261
- Ligands
- LMR, MLT
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetrahydromethanopterin S-methyltransferase subunit a (EC 2.1.1.86) | protein | 172 | 30% helix, 15% strand | Q58261 |
| B | Tetrahydromethanopterin S-methyltransferase subunit a (EC 2.1.1.86) | protein | 172 | 30% helix, 15% strand | Q58261 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.63 | 0.84 | 27 | LMR |
| 2 | 90 | 0.56 | 0.86 | 20 | MLT |
Interfaces
1 interface between chains.
- A–B · 496 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 5L8X · X-ray structure of apo methanocaldococcus jannaschii methyltransferase subunit a at 1.85… · the same entry in another collection · chain A against A, TM-score 1.00
- Q58261 · AlphaFold monomer V2.0 prediction for tetrahydromethanopterin S-methyltransferase subunit… · 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 Q58261
- Elsewhere: RCSB PDB 5L8X · PDBe 5L8X · UniProt Q58261
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