Research workbench
Structural basis for targeted P97 remodeling by aspl as prerequisite for P97 trimethylation by METTL21D
Analyse Structural basis for targeted P97 remodeling by aspl as prerequisite for P97… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OAS
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- UniProt
- F4HUD6
- Ligands
- SAH
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-adenosyl-L-methionine-dependent methyltransferases superfamily protein | protein | 216 | 38% helix, 28% strand | F4HUD6 |
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 | 155 | 0.62 | 0.84 | 27 | SAH |
Compared structures
- 7OAS · Structural basis for targeted p97 remodeling by ASPL as prerequisite for p97… · 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 F4HUD6
- Elsewhere: RCSB PDB 7OAS · PDBe 7OAS · UniProt F4HUD6
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