Research workbench
Crystal structure of mmtn
Analyse Crystal structure of mmtn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VVV
- Type
- protein
- Length
- 811 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SAM-dependent methyltransferase
- UniProt
- A0A0T5PCK9
- Ligands
- PO4
- Pockets
- 12 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SAM-dependent methyltransferase | protein | 280 | 41% helix, 18% strand | A0A0T5PCK9 |
| B | SAM-dependent methyltransferase | protein | 258 | 34% helix, 20% strand | A0A0T5PCK9 |
| C | SAM-dependent methyltransferase | protein | 273 | 37% helix, 18% strand | A0A0T5PCK9 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 859 | 0.82 | 0.84 | 75 | empty |
| 2 | 623 | 0.75 | 0.82 | 52 | empty |
| 3 | 414 | 0.65 | 0.79 | 59 | empty |
| 4 | 231 | 0.61 | 0.81 | 36 | PO4 |
| 5 | 274 | 0.55 | 0.76 | 28 | empty |
Interfaces
3 interfaces between chains.
- A–B · 937 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 885 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 874 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7VVV · Crystal structure of MmtN · 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 A0A0T5PCK9
- Elsewhere: RCSB PDB 7VVV · PDBe 7VVV · UniProt A0A0T5PCK9
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