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: 7ZEX
Type: protein + RNA
Length: 101 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isoform 3 of peptidyl-prolyl cis-trans isomerase E; RNA (5'-R(*UP*AP*AP*UP*GP*UP*CP*G)-3')
EC: 5.2.1.8
UniProt: Q9UNP9

Structure

solution nmr · 2 distinct chains · 24% helix, 25% 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, 25% strand	Q9UNP9
B	RNA (5'-R(UPAPAPUPGPUPCPG)-3')	rna	8	—	—

Interfaces

1 interface between chains.

A–B · 1060 Å² buried · 37 hydrogen bonds · protein-nucleic

Compared structures

7ZEX · Complex Cyp33-RRMdelta alpha : UAAUGUCG RNA · 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 0.84

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
Elsewhere: RCSB PDB 7ZEX · PDBe 7ZEX · UniProt Q9UNP9

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.