Research workbench
Complex between BD1 of BRD3 and gata-1 C-tail
Analyse Complex between BD1 of BRD3 and gata-1 C-tail in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2L5E
- Type
- protein
- Length
- 133 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain-containing protein 3; Gata-1
- UniProt
- Q3TUI3
Structure
solution nmr · 2 distinct chains · 47% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bromodomain-containing protein 3 | protein | 127 | 49% helix, 2% strand | Q3TUI3 |
| B | Gata-1 | protein | 6 | 0% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 444 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (acetylation).
Compared structures
- 2L5E · Complex between BD1 of Brd3 and GATA-1 C-tail · the same entry in another collection · chain A against A, TM-score 1.00
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 Q3TUI3
- Elsewhere: RCSB PDB 2L5E · PDBe 2L5E · UniProt Q3TUI3
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