MolNFT v1 · #100647 · protein
Crystal structure of the bromodomain-phd finger module of human transcriptional co-activator cbp in complex with acetylated histone 4 peptide (H4K20AC).
4N3W · Creb-binding protein: “Crystal structure of the bromodomain-phd finger module of human transcriptional co-activator cbp in complex…”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.40). MolNFT v1 #100647 on…
- PDB
- 4N3W
- Type
- protein
- Length
- 189 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Creb-binding protein; Histone H4 peptide
- EC
- 2.3.1.48
- UniProt
- Q92793
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Creb-binding protein (EC 2.3.1.48) | protein | 184 | 42% helix, 4% strand | Q92793 |
| C | Histone H4 peptide | protein | 5 | 0% helix, 0% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.40 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–C · 509 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 4N3W · Crystal Structure of the Bromodomain-PHD Finger Module of Human Transcriptional… · the same entry in another collection · chain A against A, TM-score 1.00
- Q92793 · AlphaFold monomer V2.0 prediction for creb-binding protein (Q92793) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 Q92793
- Elsewhere: RCSB PDB 4N3W · PDBe 4N3W · UniProt Q92793
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