Research workbench
Crystal structure of the plantazolicin methyltransferase baml in complex with sah
Analyse Crystal structure of the plantazolicin methyltransferase baml in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KVZ
- Type
- protein
- Length
- 269 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Baml
- EC
- 2.1.1.-
- UniProt
- D3VMM1
- Ligands
- SAH
- Pockets
- 1 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Baml (EC 2.1.1.-) | protein | 269 | 51% helix, 19% strand | D3VMM1 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
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 | 526 | 0.80 | 0.86 | 75 | SAH |
Compared structures
- 4KVZ · Crystal structure of the plantazolicin methyltransferase BamL in complex with SAH · 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 D3VMM1
- Elsewhere: RCSB PDB 4KVZ · PDBe 4KVZ · UniProt D3VMM1
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