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Crystal structure of HNRNPA2B1 in complex with RNA

Analyse Crystal structure of HNRNPA2B1 in complex with RNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EN1
Type: protein + RNA
Length: 191 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heterogeneous nuclear ribonucleoproteins A2/B1; RNA (5'-R(*AP*GP*GP*AP*CP*UP*G)-3')
UniProt: P22626
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heterogeneous nuclear ribonucleoproteins A2/B1	protein	184	25% helix, 35% strand	P22626
B	RNA (5'-R(APGPGPAPCPUP*G)-3')	rna	7	—	—

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	275	0.64	0.81	28	empty

Interfaces

1 interface between chains.

A–B · 551 Å² buried · 12 hydrogen bonds · protein-nucleic

Compared structures

5EN1 · Crystal structure of hnRNPA2B1 in complex with RNA · the same entry in another collection · chain A against A, TM-score 1.00
P22626 · AlphaFold monomer V2.0 prediction for heterogeneous nuclear ribonucleoproteins A2/B1… · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P22626
Elsewhere: RCSB PDB 5EN1 · PDBe 5EN1 · UniProt P22626

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