Research workbench
Crystal structure of erks in complex with 5-CHLOROBENZO[D]OXAZOL-2- amine
Analyse Crystal structure of erks in complex with 5-CHLOROBENZO[D]OXAZOL-2- amine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QP2
- Type
- protein
- Length
- 667 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 1
- EC
- 2.7.11.24
- UniProt
- P28482
- Ligands
- 36R
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 1 (EC 2.7.11.24) | protein | 337 | 39% helix, 16% strand | P28482 |
| B | Mitogen-activated protein kinase 1 (EC 2.7.11.24) | protein | 330 | 35% helix, 15% strand | P28482 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1059 | 0.76 | 0.78 | 82 | empty |
| 2 | 218 | 0.68 | 0.85 | 30 | empty |
| 3 | 299 | 0.66 | 0.82 | 35 | 36R, IMD |
| 4 | 289 | 0.58 | 0.78 | 27 | empty |
| 5 | 261 | 0.57 | 0.77 | 43 | empty |
Interfaces
1 interface between chains.
- A–B · 795 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 4QP2 · Crystal Structure of ERKs in complex with 5-chlorobenzo[d]oxazol-2-amine · the same entry in another collection · chain A against A, TM-score 1.00
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 P28482
- Elsewhere: RCSB PDB 4QP2 · PDBe 4QP2 · UniProt P28482
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