MolNFT v1 · #117855 · protein
Crystal structure of MAPK13 complex with inhibitor
5EKN · Mitogen-activated protein kinase 13: “Crystal structure of MAPK13 complex with inhibitor”. X-ray diffraction, 1 ligand (N58), 1 pocket (best druggability 0.74). MolNFT v1 #117855 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 5EKN
- Type
- protein
- Length
- 336 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 13
- EC
- 2.7.11.24
- UniProt
- O15264
- Ligands
- N58
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 13 (EC 2.7.11.24) | protein | 336 | 37% helix, 15% strand | O15264 |
Ligands and binding sites
- N58 · 1-(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)-3-[4-(pyridin-4-ylsulfanyl)phenyl]urea · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 526 | 0.74 | 0.82 | 46 | N58 |
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 O15264
- Elsewhere: RCSB PDB 5EKN · PDBe 5EKN · UniProt O15264
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