MolNFT v1 · #156932 · protein
Structure of dbophma in complex with sah and methylated peptide
6MJG · Fusion protein of dbophma and methylated peptide: “Structure of dbophma in complex with sah and methylated peptide”. X-ray diffraction, 2 ligands (SAH, ZN), 3 pockets (best druggability 0.79). MolNFT v1 #156932 on GenesisL1: 3D…
- PDB
- 6MJG
- Type
- protein
- Length
- 386 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusion protein of dbophma and methylated peptide
- Ligands
- SAH, ZN
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fusion protein of dbophma and methylated peptide | protein | 386 | 41% helix, 14% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.79 | 0.98 | 23 | SAH |
| 2 | 106 | 0.37 | 0.74 | 19 | empty |
| 3 | 81 | 0.33 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 4 modified (methylation, nonstandard).
Compared structures
- 6MJG · Structure of dbOphMA in Complex with SAH and Methylated Peptide · 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 6MJG · PDBe 6MJG
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