Research workbench
CA2+-bound mthk rck domain at 2.5 ångström
Analyse CA2+-bound mthk rck domain at 2.5 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L73
- Type
- protein
- Length
- 446 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium-gated potassium channel mthk
- UniProt
- O27564
- Ligands
- NA, CA, CL
- Pockets
- 7 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calcium-gated potassium channel mthk | protein | 224 | 38% helix, 23% strand | O27564 |
| B | Calcium-gated potassium channel mthk | protein | 222 | 40% helix, 23% strand | O27564 |
Ligands and binding sites
- NA · Sodium ion · metal · 8 copies · chains A, B
- CA · Calcium ion · metal · 5 copies · chains A, B
- CL · Chloride ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 307 | 0.75 | 0.87 | 42 | empty |
| 2 | 162 | 0.48 | 0.77 | 27 | empty |
| 3 | 143 | 0.43 | 0.75 | 28 | empty |
| 4 | 132 | 0.40 | 0.74 | 24 | CA |
| 5 | 98 | 0.33 | 0.73 | 16 | CA |
Interfaces
1 interface between chains.
- A–B · 3640 Ų buried · 50 hydrogen bonds · protein-protein
Compared structures
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 O27564
- Elsewhere: RCSB PDB 4L73 · PDBe 4L73 · UniProt O27564
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