Research workbench
BRD2-BD1 in complex with the cyclic peptide 4.2_3
Analyse BRD2-BD1 in complex with the cyclic peptide 4.2_3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ULQ
- Type
- protein
- Length
- 416 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- H0Y6K2
- Ligands
- ACE
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 126 | — | H0Y6K2 |
| B | — | protein | 127 | — | H0Y6K2 |
| C | — | protein | 118 | — | H0Y6K2 |
| D, E, F | — | protein | 15 | — | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 3 copies · chains A, D, C, E, B, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6ULQ · BRD2-BD1 in complex with the cyclic peptide 4.2_3 · 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 H0Y6K2
- Elsewhere: RCSB PDB 6ULQ · PDBe 6ULQ · UniProt H0Y6K2
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