4ED5: Two N-terminal RRM domains of HuR

Crystal structure of the two N-terminal RRM domains of HuR complexed with RNA. Determined by X-ray diffraction at 2.0 Å resolution. Released 23 May 2012.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
4
Atoms
3,220
Mol. weight
47.27 kDa
Ligands
M2M
Released
23 May 2012

Explore 4ED5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ED5 contains 17 α-helices and 20 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand21-2551
α-helix33-419
β-strand46-5381
β-strand60-6891
α-helix71-8111
β-strand85-8622
β-strand89-9022
β-strand92-9541
α-helix96-994
α-helix101-1033
β-strand107-11153
α-helix119-1268
α-helix127-1293
β-strand132-13983
β-strand146-15493
α-helix157-16711
α-helix171-1722
α-helix178-1792
β-strand180-18343
Chain B: 8 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand21-2554
α-helix33-419
β-strand46-5384
β-strand60-6894
α-helix71-8111
β-strand85-8625
β-strand89-9025
β-strand92-9544
α-helix96-994
β-strand107-11156
α-helix119-1268
α-helix127-1293
β-strand132-13986
β-strand146-15496
α-helix157-16711
α-helix170-1723
α-helix178-1792
β-strand180-18346

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ELAV-like protein 1A, Bprotein177Homo sapiensQ15717 (AlphaFold model)
5'-r(*a*up*up*up*up*up*ap*up*up*up*u)-3'C, DRNA11
Sequence of entity 1 (A, B), FASTA
>4ED5_1 ELAV-like protein 1 (chains A, B)
GRTNLIVNYLPQNMTQDELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYVTAKDAERA
INTLNGLRLQSKTIKVSYARPSSEVIKDANLYISGLPRTMTQKDVEDMFSRFGRIINSRV
LVDQTTGLSRGVAFIRFDKRSEAEEAITSFNGHKPPGSSEPITVKFAANLEHHHHHH
Sequence of entity 2 (C, D), FASTA
>4ED5_2 5'-R(*A*UP*UP*UP*UP*UP*AP*UP*UP*UP*U)-3' (chains C, D)
AUUUUUAUUUU

Ligands and cofactors

IDNameFormulaCopies
M2M1-methoxy-2-(2-methoxyethoxy)ethaneC6 H14 O31

Water and common crystallization additives (EDO, GOL) are not listed.

Primary citation

The structure of the ARE-binding domains of Hu antigen R (HuR) undergoes conformational changes during RNA binding. Wang, H., Zeng, F., Liu, Q. et al. Acta Crystallogr D Biol Crystallogr (2013) 69:373-380. DOI 10.1107/S0907444912047828 · PubMed

Other PDB entries of the same protein (UniProt Q15717 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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