Research workbench
1.6 ångström crystal structure of the alpha-kinase domain of myosin heavy chain kinase a complex with AMP
Analyse 1.6 ångström crystal structure of the alpha-kinase domain of myosin heavy chain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LKM
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin heavy chain kinase a
- EC
- 2.7.11.7
- UniProt
- P42527
- Ligands
- AMP, MG, ZN, PO4
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin heavy chain kinase a (EC 2.7.11.7) | protein | 247 | 24% helix, 29% strand | P42527 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
- MG · Magnesium ion · metal · 3 copies · chains A
- ZN · Zinc ion · metal · chains A
- PO4 · Phosphate ion · ion · 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 | 236 | 0.62 | 0.81 | 39 | MG, PO4, AMP |
| 2 | 129 | 0.41 | 0.75 | 18 | empty |
Compared structures
- 3LKM · 1.6 Angstrom Crystal Structure of the Alpha-kinase Domain of Myosin Heavy Chain Kinase A… · the same entry in another collection · chain A against A, TM-score 1.00
- P42527 · AlphaFold monomer V2.0 prediction for myosin heavy chain kinase a (P42527) · a predicted model of the same protein · chain A against A, TM-score 0.81
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 P42527
- Elsewhere: RCSB PDB 3LKM · PDBe 3LKM · UniProt P42527
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