MolNFT v1 · #41541 · protein
NMR structure of the yeast DUN1 fha domain in complex with a doubly phosphorylated (pt) peptide derived from RAD53 SCD1
2JQL · DNA damage response protein kinase DUN1: “NMR structure of the yeast DUN1 fha domain in complex with a doubly phosphorylated (pt) peptide derived from…”. Solution nmr, 2 pockets (best druggability 0.26). MolNFT v1 #41541 on…
- PDB
- 2JQL
- Type
- protein
- Length
- 151 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA damage response protein kinase DUN1; SERINE/THREONINE-protein kinase RAD53
- EC
- 2.7.11.1
- UniProt
- P39009, P22216
- Pockets
- 2 · best druggability 0.26
Structure
solution nmr · 2 distinct chains · 0% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA damage response protein kinase DUN1 (EC 2.7.11.1) | protein | 141 | 0% helix, 45% strand | P39009 |
| B | SERINE/THREONINE-protein kinase RAD53 (EC 2.7.11.1) | protein | 10 | 0% helix, 0% strand | P22216 |
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 | 50 | 0.26 | 0.74 | 16 | empty |
| 2 | 50 | 0.25 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 546 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 2JQL · NMR structure of the yeast Dun1 FHA domain in complex with a doubly phosphorylated (pT)… · the same entry in another collection · chain B against B, TM-score 1.00
- P39009 · AlphaFold monomer V2.0 prediction for DNA damage response protein kinase DUN1 (P39009) · a predicted model of the same protein · chain A against A, TM-score 0.72
- P22216 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase RAD53 (P22216) · a predicted model of the same protein · chain B against A, TM-score 0.44
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 P39009
- Every structure of UniProt P22216
- Elsewhere: RCSB PDB 2JQL · PDBe 2JQL · UniProt P39009 · UniProt P22216
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