Research workbench
Fragment-based discovery of protein-protein interaction inhibitors of replication protein a
Analyse Fragment-based discovery of protein-protein interaction inhibitors of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IJL
- Type
- protein
- Length
- 122 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Replication protein a 70 kda DNA-binding subunit
- UniProt
- P27694
- Ligands
- 1EK
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Replication protein a 70 kda DNA-binding subunit | protein | 122 | 19% helix, 41% strand | P27694 |
Ligands and binding sites
- 1EK · {[5-(3-chloro-1-benzothiophen-2-yl)-4-phenyl-4H-1,2,4-triazol-3-yl]sulfanyl}acetic acid · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4IJL · Fragment-based Discovery of Protein-Protein Interaction Inhibitors of Replication Protein… · the same entry in another collection · chain A against A, TM-score 1.00
- P27694 · AlphaFold monomer V2.0 prediction for replication protein a 70 kda DNA-binding subunit… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P27694
- Elsewhere: RCSB PDB 4IJL · PDBe 4IJL · UniProt P27694
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.