Research workbench
SAM complex with akmt from the hyperthermophilic archaeon sulfolobus islandicu
Analyse SAM complex with akmt from the hyperthermophilic archaeon sulfolobus islandicu in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FA8
- Type
- protein
- Length
- 156 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribosomal protein L11 methyltransferase, putative
- UniProt
- C3MWA1
- Ligands
- SAM, MG
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosomal protein L11 methyltransferase, putative | protein | 156 | 30% helix, 26% strand | C3MWA1 |
Ligands and binding sites
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 | 220 | 0.57 | 0.79 | 29 | SAM |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 5FA8 · SAM complex with aKMT from the hyperthermophilic archaeon Sulfolobus islandicu · 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 C3MWA1
- Elsewhere: RCSB PDB 5FA8 · PDBe 5FA8 · UniProt C3MWA1
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