MolNFT v1 · #11971 · protein
Solution structure of the FHA2 domain of RAD53 complexed with a phosphotyrosyl peptide derived from RAD9
1K2M · Protein kinase SPK1: “Solution structure of the FHA2 domain of RAD53 complexed with a phosphotyrosyl peptide derived from RAD9”. Solution nmr, 1 pocket (best druggability 0.35). MolNFT v1 #11971 on GenesisL1: 3D structure, binding…
- PDB
- 1K2M
- Type
- protein
- Length
- 165 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein kinase SPK1; DNA repair protein RAD9
- EC
- 2.7.1.-
- UniProt
- P22216, P14737
- Pockets
- 1 · best druggability 0.35
Structure
solution nmr · 2 distinct chains · 5% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein kinase SPK1 (EC 2.7.1.-) | protein | 158 | 5% helix, 34% strand | P22216 |
| P | DNA repair protein RAD9 | protein | 7 | 0% helix, 0% strand | P14737 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.35 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–P · 385 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 1K2M · Solution Structure of the FHA2 Domain of Rad53 Complexed with a Phosphotyrosyl Peptide… · the same entry in another collection · chain A against A, TM-score 1.00
- P22216 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase RAD53 (P22216) · a predicted model of the same protein · chain A against A, TM-score 0.83
- P14737 · AlphaFold monomer V2.0 prediction for DNA repair protein RAD9 (P14737) · a predicted model of the same protein · chain P against A, TM-score 0.60
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 P22216
- Every structure of UniProt P14737
- Elsewhere: RCSB PDB 1K2M · PDBe 1K2M · UniProt P22216 · UniProt P14737
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