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Structure of ADP-bound human NEK7
Analyse Structure of ADP-bound human NEK7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WQN
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase NEK7
- EC
- 2.7.11.1
- UniProt
- Q8TDX7
- Ligands
- ADP, NI, MG, SO4
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase NEK7 (EC 2.7.11.1) | protein | 259 | 42% helix, 18% strand | Q8TDX7 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- NI · Nickel (II) ion · metal · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · 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 | 302 | 0.55 | 0.75 | 40 | ADP |
| 2 | 65 | 0.42 | 0.80 | 16 | empty |
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 Q8TDX7
- Elsewhere: RCSB PDB 2WQN · PDBe 2WQN · UniProt Q8TDX7
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