MolNFT v1 · #118105 · protein
Crystal structure of microtubule affinity-regulating kinase 4 catalytic domain in complex with a pyrazolopyrimidine inhibitor
5ES1 · MAP/MICROTUBULE affinity-regulating kinase 4: “Crystal structure of microtubule affinity-regulating kinase 4 catalytic domain in complex with a…”. X-ray diffraction, 1 ligand (5RC), 4 pockets (best druggability 0.68). MolNFT v1…
- PDB
- 5ES1
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MAP/MICROTUBULE affinity-regulating kinase 4
- EC
- 2.7.11.1
- UniProt
- Q96L34
- Ligands
- 5RC
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MAP/MICROTUBULE affinity-regulating kinase 4 (EC 2.7.11.1) | protein | 304 | 40% helix, 15% strand | Q96L34 |
Ligands and binding sites
- 5RC · ~{N}-[(1~{R},6~{R})-6-azanyl-2,2-bis(fluoranyl)cyclohexyl]-5-ethyl-4-[6-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-3-yl]thiophene-2-carboxamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 369 | 0.68 | 0.81 | 45 | 5RC |
| 2 | 322 | 0.54 | 0.75 | 40 | empty |
| 3 | 103 | 0.37 | 0.75 | 21 | empty |
| 4 | 50 | 0.23 | 0.72 | 13 | empty |
Compared structures
- 5ES1 · Crystal structure of microtubule affinity-regulating kinase 4 catalytic domain in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- Q96L34 · AlphaFold monomer V2.0 prediction for MAP/MICROTUBULE affinity- regulating kinase 4… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q96L34
- Elsewhere: RCSB PDB 5ES1 · PDBe 5ES1 · UniProt Q96L34
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