Research workbench
Crystal structure of the pumilio-homology domain from human PUMILIO1 in complex with P38ALPHA nreb
Analyse Crystal structure of the pumilio-homology domain from human PUMILIO1 in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3Q0M
- Type
- protein + RNA
- Length
- 691 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pumilio homolog 1; 5'-R(UP*GP*UP*AP*GP*AP*UP*A)-3'
- UniProt
- Q14671
- Pockets
- 4 · best druggability 0.59
Structure
x-ray diffraction · 3 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pumilio homolog 1 | protein | 337 | 69% helix, 0% strand | Q14671 |
| B | Pumilio homolog 1 | protein | 338 | 70% helix, 0% strand | Q14671 |
| C, D | 5'-R(UP*GP*UP*AP*GP*AP*UP*A)-3' | rna | 8 | — | — |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.59 | 0.80 | 33 | empty |
| 2 | 218 | 0.47 | 0.74 | 33 | empty |
| 3 | 58 | 0.34 | 0.78 | 13 | empty |
| 4 | 56 | 0.33 | 0.78 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1403 Ų buried · 46 hydrogen bonds · protein-nucleic
- B–D · 1378 Ų buried · 46 hydrogen bonds · protein-nucleic
- A–B · 312 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3Q0M · Crystal structure of the PUMILIO-homology domain from Human PUMILIO1 in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q14671 · AlphaFold monomer V2.0 prediction for pumilio homolog 1 (Q14671) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q14671
- Elsewhere: RCSB PDB 3Q0M · PDBe 3Q0M · UniProt Q14671
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