Research workbench
Crystal structure of a calmodulin-lysine N-methyltransferase fragment
Analyse Crystal structure of a calmodulin-lysine N-methyltransferase fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PWY
- Type
- protein
- Length
- 250 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin-lysine N-methyltransferase
- EC
- 2.1.1.60
- UniProt
- Q7Z624
- Ligands
- SAH, UNX
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin-lysine N-methyltransferase (EC 2.1.1.60) | protein | 250 | 38% helix, 25% strand | Q7Z624 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
- UNX · Unknown atom or ion · ion · 19 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- MLI · Malonate ion · additive · 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 | 184 | 0.51 | 0.77 | 24 | SAH, GOL |
| 2 | 189 | 0.50 | 0.76 | 32 | UNX |
Compared structures
- 4PWY · Crystal structure of a Calmodulin-lysine N-methyltransferase fragment · the same entry in another collection · chain A against A, TM-score 1.00
- Q7Z624 · AlphaFold monomer V2.0 prediction for calmodulin-lysine N-methyltransferase (Q7Z624) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q7Z624
- Elsewhere: RCSB PDB 4PWY · PDBe 4PWY · UniProt Q7Z624
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