Research workbench
Phage SAM lyase in complex with S-adenosyl-L-homocysteine
Analyse Phage SAM lyase in complex with S-adenosyl-L-homocysteine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZMG
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.48
- Source
- unidentified
- Molecule
- Chains: A
- Ligands
- SAH, PO4
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · resolution 1.48 · 1 distinct chain · 26% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chains: A | protein | 129 | 26% helix, 40% strand | — |
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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.48 | 0.80 | 23 | SAH |
Compared structures
- 6ZMG · Phage SAM lyase in complex with S-adenosyl-L-homocysteine · 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
- Elsewhere: RCSB PDB 6ZMG · PDBe 6ZMG
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