Research workbench
Mechanism of creb recognition and coactivation by the creb regulated transcriptional coactivator CRTC2
Analyse Mechanism of creb recognition and coactivation by the creb regulated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HTM
- Type
- protein
- Length
- 28 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Creb-regulated transcription coactivator 2
- UniProt
- Q53ET0
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 89% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Creb-regulated transcription coactivator 2 | protein | 28 | 89% helix, 0% strand | Q53ET0 |
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.
Compared structures
- 4HTM · Mechanism of CREB Recognition and Coactivation by the CREB Regulated Transcriptional… · the same entry in another collection · chain A against A, TM-score 1.00
- Q53ET0 · AlphaFold monomer V2.0 prediction for creb-regulated transcription coactivator 2 (Q53ET0) · 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 Q53ET0
- Elsewhere: RCSB PDB 4HTM · PDBe 4HTM · UniProt Q53ET0
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