MolNFT v1 · #136605 · protein
Prolyl isomerase PIN1 R14A mutant bound with BRD4 peptide
5UY9 · Peptidyl-prolyl cis-trans isomerase nima-interacting 1: “Prolyl isomerase PIN1 R14A mutant bound with BRD4 peptide”. X-ray diffraction, 2 ligands (NIT, SO4), 2 pockets (best druggability 0.37). MolNFT v1 #136605 on GenesisL1: 3D…
- PDB
- 5UY9
- Type
- protein
- Length
- 152 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase nima-interacting 1; BRD4 peptide
- EC
- 5.2.1.8
- UniProt
- Q13526
- Ligands
- NIT, SO4
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase nima-interacting 1 (EC 5.2.1.8) | protein | 146 | 27% helix, 27% strand | Q13526 |
| B | BRD4 peptide | protein | 6 | 0% helix, 0% strand | — |
Ligands and binding sites
- NIT · 4-nitroaniline · ligand · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- PE4 · 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.37 | 0.79 | 20 | NIT, SO4 |
| 2 | 50 | 0.29 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 385 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, phosphorylation).
Compared structures
- 5UY9 · Prolyl isomerase Pin1 R14A mutant bound with Brd4 peptide · 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 Q13526
- Elsewhere: RCSB PDB 5UY9 · PDBe 5UY9 · UniProt Q13526
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