Research workbench
Crystal structure of P300 CH1 domain in complex with citif (a CITED2- hif-1ALPHA hybrid)
Analyse Crystal structure of P300 CH1 domain in complex with citif (a CITED2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QGS
- Type
- protein
- Length
- 148 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CBP/P300-interacting transactivator 2,HYPOXIA-inducible factor 1-alpha; Histone…
- EC
- 2.3.1.48
- UniProt
- Q99967, Q16665, Q7Z6C1
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | CBP/P300-interacting transactivator 2,HYPOXIA-inducible factor 1-alpha | protein | 55 | 40% helix, 0% strand | Q99967, Q16665 |
| A | Histone acetyltransferase (EC 2.3.1.48) | protein | 93 | 63% helix, 0% strand | Q7Z6C1 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- B–A · 2331 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 7QGS · Crystal structure of p300 CH1 domain in complex with CITIF (a CITED2-HIF-1alpha hybrid) · the same entry in another collection · chain B against B, TM-score 1.00
- Q99967 · AlphaFold monomer V2.0 prediction for CBP/P300-interacting transactivator 2 (Q99967) · a predicted model of the same protein · chain B against A, TM-score 0.44
- Q16665 · AlphaFold monomer V2.0 prediction for hypoxia-inducible factor 1-alpha (Q16665) · a predicted model of the same protein · chain B against A, TM-score 0.36
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 Q99967
- Every structure of UniProt Q16665
- Every structure of UniProt Q7Z6C1
- Elsewhere: RCSB PDB 7QGS · PDBe 7QGS · UniProt Q99967 · UniProt Q16665 · UniProt Q7Z6C1
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