Research workbench
BRD2-BD2 in complex with the cyclic peptide 4.2_3
Analyse BRD2-BD2 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
- 6ULT
- Type
- protein
- Length
- 889 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25440
- Ligands
- ACE
Structure
x-ray diffraction · 10 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 104 | — | P25440 |
| B, F, H | — | protein | 108 | — | P25440 |
| C | — | protein | 101 | — | P25440 |
| D | — | protein | 107 | — | P25440 |
| E | — | protein | 109 | — | P25440 |
| G | — | protein | 102 | — | P25440 |
| I | — | protein | 12 | — | — |
| J | — | protein | 10 | — | — |
| K | — | protein | 11 | — | — |
| L | — | protein | 9 | — | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 4 copies · chains H, I, E, J, A, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6ULT · BRD2-BD2 in complex with the cyclic peptide 4.2_3 · the same entry in another collection · chain L against L, 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 P25440
- Elsewhere: RCSB PDB 6ULT · PDBe 6ULT · UniProt P25440
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.