MolNFT v1 · #86517 · protein
Crystal structure of human MPS1 tpr domain
4B94 · Dual specificity protein kinase ttk: “Crystal structure of human MPS1 tpr domain”. X-ray diffraction, 7 pockets (best druggability 0.73). MolNFT v1 #86517 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4B94
- Type
- protein
- Length
- 556 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity protein kinase ttk
- EC
- 2.7.12.1
- UniProt
- P33981
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Dual specificity protein kinase ttk (EC 2.7.12.1) | protein | 141 | 73% helix, 1% strand | P33981 |
| B, C | Dual specificity protein kinase ttk (EC 2.7.12.1) | protein | 137 | 76% helix, 1% strand | P33981 |
Ligands and binding sites
- GOL · Glycerol · additive · 10 copies · chains A, C, B, D
- PG4 · Tetraethylene glycol · additive · 2 copies · chains A, C, B, D
- PGE · Triethylene glycol · additive · 2 copies · chains B, C
- MLI · Malonate ion · additive · 2 copies · chains B, D, A
- PEG · Di(hydroxyethyl)ether · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 828 | 0.73 | 0.78 | 67 | GOL, MLI |
| 2 | 781 | 0.73 | 0.78 | 51 | empty |
| 3 | 97 | 0.37 | 0.75 | 15 | empty |
| 4 | 104 | 0.36 | 0.74 | 23 | empty |
| 5 | 83 | 0.34 | 0.75 | 17 | empty |
Interfaces
5 interfaces between chains.
- B–D · 1070 Ų buried · 26 hydrogen bonds · protein-protein
- A–C · 981 Ų buried · 18 hydrogen bonds · protein-protein
- A–D · 681 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 70 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 45 Ų buried · 0 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 P33981
- Elsewhere: RCSB PDB 4B94 · PDBe 4B94 · UniProt P33981
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