Research workbench
Crystal structure of RAD4 BRCT1,2 in complex with a SLD3 phosphopeptide
Analyse Crystal structure of RAD4 BRCT1,2 in complex with a SLD3 phosphopeptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HM3
- Type
- protein
- Length
- 208 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-M checkpoint control protein RAD4; DNA replication regulator SLD3
- UniProt
- P32372, Q09761
- Ligands
- CA
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-M checkpoint control protein RAD4 | protein | 183 | 37% helix, 17% strand | P32372 |
| B | DNA replication regulator SLD3 | protein | 25 | 0% helix, 12% strand | Q09761 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 50 | 0.29 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 501 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 6HM3 · Crystal structure of Rad4 BRCT1,2 in complex with a Sld3 phosphopeptide · the same entry in another collection · chain A against A, TM-score 1.00
- P32372 · AlphaFold monomer V2.0 prediction for S-M checkpoint control protein RAD4 (P32372) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q09761 · AlphaFold monomer V2.0 prediction for DNA replication regulator SLD3 (Q09761) · a predicted model of the same protein · chain B against A, TM-score 0.24
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 P32372
- Every structure of UniProt Q09761
- Elsewhere: RCSB PDB 6HM3 · PDBe 6HM3 · UniProt P32372 · UniProt Q09761
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