Research workbench
Crystal structure of methyltransferase CALO6
Analyse Crystal structure of methyltransferase CALO6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Z2Y
- Type
- protein
- Length
- 299 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CALO6
- UniProt
- Q8KND2
- Ligands
- HG
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CALO6 | protein | 299 | 35% helix, 12% strand | Q8KND2 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 340 | 0.56 | 0.75 | 55 | empty |
| 2 | 211 | 0.45 | 0.73 | 29 | HG |
Compared structures
- 4Z2Y · Crystal structure of methyltransferase CalO6 · 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 Q8KND2
- Elsewhere: RCSB PDB 4Z2Y · PDBe 4Z2Y · UniProt Q8KND2
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