Research workbench
Mitogen activated protein kinase 7 in complex with inhibitor
Analyse Mitogen activated protein kinase 7 in complex with inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZSL
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 7
- EC
- 2.7.11.24
- UniProt
- Q13164
- Ligands
- 4QZ
- Pockets
- 5 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 7 (EC 2.7.11.24) | protein | 341 | 45% helix, 13% strand | Q13164 |
Ligands and binding sites
- 4QZ · 3-amino-5-[(4-chlorophenyl)amino]-N-[(1S)-1-phenylethyl]-1H-1,2,4-triazole-1-carboxamide · ligand · chains A
- GOL · Glycerol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 100 | 0.57 | 0.85 | 15 | 4QZ |
| 2 | 52 | 0.50 | 0.87 | 15 | empty |
| 3 | 115 | 0.40 | 0.76 | 23 | empty |
| 4 | 60 | 0.28 | 0.73 | 15 | empty |
| 5 | 50 | 0.26 | 0.74 | 16 | empty |
Compared structures
- 4ZSL · Mitogen activated protein kinase 7 in complex with inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- Q13164 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase 7 (Q13164) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q13164
- Elsewhere: RCSB PDB 4ZSL · PDBe 4ZSL · UniProt Q13164
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