Research workbench
RNA binding induces an allosteric switch in CYP33 to repress MLL1 mediated transcription regulation
Analyse RNA binding induces an allosteric switch in CYP33 to repress MLL1 mediated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ZEZ
- Type
- protein
- Length
- 170 residues
- Chains
- 3
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 3 of peptidyl-prolyl cis-trans isomerase E; Mll cleavage product N320; Histone H3
- EC
- 5.2.1.8
- UniProt
- Q9UNP9, Q03164, B4E380
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.42
Structure
solution nmr · 3 distinct chains · 18% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 3 of peptidyl-prolyl cis-trans isomerase E (EC 5.2.1.8) | protein | 93 | 24% helix, 30% strand | Q9UNP9 |
| B | Mll cleavage product N320 | protein | 64 | 14% helix, 13% strand | Q03164 |
| D | Histone H3 | protein | 13 | 0% helix, 8% strand | B4E380 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B
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 | 143 | 0.42 | 0.75 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–B · 909 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 718 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 43 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 7ZEZ · Trimolecular complex Cyp33-RRMdelta alpha : MLL1-PHD3 : H3K4me3 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UNP9 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase E (Q9UNP9) · a predicted model of the same protein · chain A against A, TM-score 0.79
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 Q9UNP9
- Every structure of UniProt Q03164
- Every structure of UniProt B4E380
- Elsewhere: RCSB PDB 7ZEZ · PDBe 7ZEZ · UniProt Q9UNP9 · UniProt Q03164 · UniProt B4E380
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