MolNFT v1 · #125954 · protein
Kinase domain of human greatwall
5LOH · SERINE/THREONINE-protein kinase GREATWALL,SERINE/THREONINE…: “Kinase domain of human greatwall”. X-ray diffraction, 2 ligands (STU, CL), 5 pockets (best druggability 0.73). MolNFT v1 #125954 on GenesisL1: 3D structure, binding sites…
- PDB
- 5LOH
- Type
- protein
- Length
- 498 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase GREATWALL,SERINE/THREONINE- protein kinase greatwall
- EC
- 2.7.11.1
- UniProt
- Q96GX5
- Ligands
- STU, CL
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase GREATWALL,SERINE/THREONINE- protein kinase greatwall (EC 2.7.11.1) | protein | 248 | 37% helix, 15% strand | Q96GX5 |
| B | SERINE/THREONINE-protein kinase GREATWALL,SERINE/THREONINE- protein kinase greatwall (EC 2.7.11.1) | protein | 250 | 36% helix, 15% strand | Q96GX5 |
Ligands and binding sites
- STU · Staurosporine · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 452 | 0.73 | 0.83 | 45 | CL |
| 2 | 206 | 0.56 | 0.79 | 20 | STU |
| 3 | 147 | 0.54 | 0.81 | 25 | empty |
| 4 | 209 | 0.52 | 0.77 | 25 | STU |
| 5 | 71 | 0.42 | 0.80 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 560 Ų buried · 6 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 Q96GX5
- Elsewhere: RCSB PDB 5LOH · PDBe 5LOH · UniProt Q96GX5
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