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RNA binding induces an allosteric switch in CYP33 to repress MLL1 mediated transcription

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: 7ZEY
Type: protein
Length: 181 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase E; Mll cleavage product N320
EC: 5.2.1.8
UniProt: Q9UNP9, Q03164
Ligands: ZN
Pockets: 1 · best druggability 0.31

Structure

solution nmr · 2 distinct chains · 26% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase E (EC 5.2.1.8)	protein	117	29% helix, 21% strand	Q9UNP9
B	Mll cleavage product N320	protein	64	20% helix, 13% strand	Q03164

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.31	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 1251 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

7ZEY · Complex Cyp33-RRM : MLL1-PHD3 · 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 0.68

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
Elsewhere: RCSB PDB 7ZEY · PDBe 7ZEY · UniProt Q9UNP9 · UniProt Q03164

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