Research workbench
P38(ALPHA) MAP kinase with the activation loop of ERK2
Analyse P38(ALPHA) MAP kinase with the activation loop of ERK2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QYX
- Type
- protein
- Length
- 339 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase 14,MITOGEN-activated protein kinase 1,MITOGEN-activated…
- EC
- 2.7.11.24
- UniProt
- Q16539, D2CIU1
- Pockets
- 8 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase 14,MITOGEN-activated protein kinase 1,MITOGEN-activated protein kinase 14 (EC 2.7.11.24) | protein | 339 | 39% helix, 15% strand | Q16539, D2CIU1 |
Ligands and binding sites
- BOG · octyl beta-D-glucopyranoside · additive · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 206 | 0.64 | 0.83 | 25 | BOG |
| 2 | 143 | 0.56 | 0.82 | 18 | empty |
| 3 | 152 | 0.44 | 0.75 | 20 | empty |
| 4 | 101 | 0.41 | 0.77 | 19 | empty |
| 5 | 91 | 0.37 | 0.76 | 18 | empty |
Compared structures
- 6QYX · p38(alpha) MAP kinase with the activation loop of ERK2 · 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 Q16539
- Every structure of UniProt D2CIU1
- Elsewhere: RCSB PDB 6QYX · PDBe 6QYX · UniProt Q16539 · UniProt D2CIU1
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