Research workbench
Pandda analysis group deposition FORM1 MAP kinase P38-alpha -- fragment N13611A in complex with MAP kinase P38-alpha
Analyse Pandda analysis group deposition FORM1 MAP kinase P38-alpha -- fragment N13611A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5R9X
- Type
- protein
- Length
- 346 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 14
- EC
- 2.7.11.24
- UniProt
- P47811
- Ligands
- NZ4, MG, CL, SO4
- Pockets
- 8 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 14 (EC 2.7.11.24) | protein | 346 | 40% helix, 15% strand | P47811 |
Ligands and binding sites
- NZ4 · N-(3-acetylphenyl)morpholine-4-carboxamide · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · 5 copies · chains A
- SO4 · Sulfate ion · ion · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 418 | 0.65 | 0.78 | 47 | empty |
| 2 | 62 | 0.45 | 0.83 | 14 | empty |
| 3 | 103 | 0.37 | 0.74 | 16 | empty |
| 4 | 91 | 0.36 | 0.75 | 15 | empty |
| 5 | 70 | 0.36 | 0.77 | 18 | CL |
Compared structures
- 5R9X · PanDDA analysis group deposition Form1 MAP kinase p38-alpha -- Fragment N13611a in… · 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 P47811
- Elsewhere: RCSB PDB 5R9X · PDBe 5R9X · UniProt P47811
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