5HQG: WD40 domain of Human E3 Ubiquitin Ligase COP1

WD40 domain of Human E3 Ubiquitin Ligase COP1 (RFWD2). Determined by X-ray diffraction at 2.0 Å resolution. Released 20 Apr 2016.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,594
Mol. weight: 40.95 kDa
Released: 20 Apr 2016

Explore 5HQG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5HQG contains 2 α-helices and 29 β-strands across 1 chain. 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: 2 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	392-399	8
β-strand	405-412	8	1
β-strand	424-429	6	2
β-strand	435-440	6	2
β-strand	444-449	6	2
α-helix	450-453	4
β-strand	465-468	4	2
β-strand	473-478	6	3
β-strand	485-490	6	3
β-strand	495-499	5	3
β-strand	505-509	5	3
β-strand	516-521	6	4
β-strand	528-533	6	4
β-strand	537-542	6	4
β-strand	550-553	4	4
β-strand	558-563	6	5
β-strand	570-575	6	5
β-strand	580-584	5	5
β-strand	587	1	5
β-strand	593-595	3	5
β-strand	602-607	6	6
β-strand	612-617	6	6
β-strand	621-626	6	6
β-strand	634-636	3	6
β-strand	648-651	4	7
β-strand	654-659	6	7
β-strand	663-668	6	7
β-strand	674-679	6	7
β-strand	700-705	6	1
β-strand	715-720	6	1
β-strand	724-730	7	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase RFWD2	A	protein	362	Homo sapiens	Q8NHY2 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5HQG_1 E3 ubiquitin-protein ligase RFWD2 (chains A)
HHHHHHMSRISDDSRTASQLDEFQECLSKFTRYNSVRPLATLSYASDLYNGSSIVSSIEF
DRDCDYFAIAGVTKKIKVYEYDTVIQDAVDIHYPENEMTCNSKISCISWSSYHKNLLASS
DYEGTVILWDGFTGQRSKVYQEHEKRCWSVDFNLMDPKLLASGSDDAKVKLWSTNLDNSV
ASIEAKANVCCVKFSPSSRYHLAFGCADHCVHYYDLRNTKQPIMVFKGHRKAVSYAKFVS
GEEIVSASTDSQLKLWNVGKPYCLRSFKGHINEKNFVGLASNGDYIACGSENNSLYLYYK
GLSKTLLTFKFDTVKSVLDKDRKEDDTNEFVSAVCWRALPDGESNVLIAANSQGTIKVLE
LV

Primary citation

Structural Basis for Substrate Selectivity of the E3 Ligase COP1. Uljon, S., Xu, X., Durzynska, I. et al. Structure (2016) 24:687-696. DOI 10.1016/j.str.2016.03.002 · PubMed

Other PDB entries of the same protein (UniProt Q8NHY2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9LTR 3.03 Å, Cryo-EM structure of dimeric DDB1-DDA1-DET1-Ube2e2-COP1 complex
9LU1 3.62 Å, protein structure of DDB1-DDA1-DET1-Ube2e2 bound to COP1 dimer
9W90 3.7 Å, DDB1-DDA1-DET1-Ube2e2-COP1-c-Jun-STK40 complex
5IGQ 3.9 Å, WD40 domain of Human E3 Ubiquitin Ligase COP1 (RFWD2) bound to peptide from Trib1
9M0Y 4.25 Å, Local refinement of stacked like DDB1-DDA1-DET1-Ube2e2-COP1 complex (layer 2)
9LUL 4.99 Å, Local refinement of stacked like DDB1-DDA1-DET1-Ube2e2-COP1 complex (layer 1)

Browse structure collections

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