Research workbench
Pandda analysis group deposition -- crystal structure of BRD1 after initial refinement with no ligand modelled (structure 104)
Analyse Pandda analysis group deposition -- crystal structure of BRD1 after initial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5PRX
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O95696
- Ligands
- NA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 121 | — | O95696 |
| B | — | protein | 123 | — | O95696 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5PRX · PanDDA analysis group deposition -- Crystal Structure of BRD1 after initial refinement… · the same entry in another collection · chain A against A, TM-score 1.00
- O95696 · AlphaFold monomer V2.0 prediction for bromodomain-containing protein 1 (O95696) · a predicted model of the same protein · chain B against A, TM-score 0.90
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 O95696
- Elsewhere: RCSB PDB 5PRX · PDBe 5PRX · UniProt O95696
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