6GD1: HuR RRM3

Structure of HuR RRM3. Determined by X-ray diffraction at 2.01 Å resolution. Released 31 Oct 2018.

Method: X-ray diffraction
Resolution: 2.01 Å
Organisms: Escherichia coli (strain K12), Homo sapiens
Chains: 2
Atoms: 3,213
Mol. weight: 45.64 kDa
Released: 31 Oct 2018

Explore 6GD1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6GD1 contains 18 α-helices and 24 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, 12 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	1
α-helix	12	1
α-helix	13-17	5
β-strand	22-28	7	1
α-helix	33-48	16
β-strand	53-59	7	1
α-helix	66-69	4
β-strand	74-75	2	2
β-strand	77-82	6	1
β-strand	85-91	7	1
α-helix	96-108	13
β-strand	114-119	6	3
α-helix	127-134	8
α-helix	135-137	3
β-strand	140-147	8	3
β-strand	154-162	9	3
α-helix	165-175	11
β-strand	179-180	2	4
β-strand	183-184	2	4
α-helix	185	1
β-strand	186-189	4	3

Chain B: 9 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	5
α-helix	12	1
α-helix	13-17	5
β-strand	23-28	6	5
α-helix	33-48	16
β-strand	54-59	6	5
α-helix	67-69	3
β-strand	74-75	2	4
β-strand	77-82	6	5
β-strand	85-91	7	5
α-helix	96-106	11
β-strand	114-119	6	6
α-helix	127-134	8
α-helix	135-137	3
β-strand	140-147	8	6
β-strand	154-162	9	6
α-helix	165-175	11
β-strand	179-180	2	2
β-strand	183-184	2	2
α-helix	185	1
β-strand	186-189	4	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Thioredoxin 1,ELAV-like protein 1	A, B	protein	206	Escherichia coli (strain K12), Homo sapiens	P0AA25 (AlphaFold model), Q15717 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6GD1_1 Thioredoxin 1,ELAV-like protein 1 (chains A, B)
MKHHHHHHPMSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQ
GKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLAGS
AMGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAM
AIASLNGYRLGDKILQVSFKTNKSHK

Primary citation

HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs. Pabis, M., Popowicz, G.M., Stehle, R. et al. Nucleic Acids Res (2019) 47:1011-1029. DOI 10.1093/nar/gky1138 · PubMed

Other PDB entries of the same protein (UniProt P0AA25 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4HUA 1.1 Å, E. coli thioredoxin variant with (4R)-FluoroPro76 as single proline residue
5HR3 1.1 Å, Crystal structure of thioredoxin N106A mutant
5HR2 1.2 Å, Crystal structure of thioredoxin L94A mutant
5HR0 1.31 Å, Crystal structure of thioredoxin E101G mutant
4HU7 1.4 Å, E. coli thioredoxin variant with Pro76 as single proline residue
4HU9 1.55 Å, E. coli thioredoxin variant with (4S)-FluoroPro76 as single proline residue
4X43 1.65 Å, Structure of proline-free E. coli Thioredoxin
2TRX 1.68 Å, Crystal structure of thioredoxin from escherichia coli at 1.68 Å resolution
6Y4Y 1.75 Å, The crystal structure of human MACROD2 in space group P41212
1KEB 1.8 Å, Crystal Structure of Double Mutant M37L,P40S E.coli Thioredoxin
2EIQ 1.9 Å, Design of Disulfide-linked Thioredoxin Dimers and Multimers Through Analysis of Crystal…
6Y4Z 1.9 Å, The crystal structure of human MACROD2 in space group P43212

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