4QPL: RNF146(RING-WWE)/UbcH5a/iso-ADPr complex

Crystal structure of RNF146(RING-WWE)/UbcH5a/iso-ADPr complex. Determined by X-ray diffraction at 1.9 Å resolution. Released 15 Oct 2014.

Method
X-ray diffraction
Resolution
1.9 Å
Organisms
Mus musculus, Homo sapiens
Chains
4
Atoms
5,333
Mol. weight
72.14 kDa
Ligands
V3L, ZN
Released
15 Oct 2014

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

Secondary structure: helices and β-sheets

4QPL contains 31 α-helices and 44 β-strands across 4 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: 7 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix33-342
β-strand3511
α-helix361
β-strand4211
β-strand46-4832
β-strand54-5632
α-helix57-648
α-helix75-784
β-strand8712
α-helix90-967
β-strand103-10973
β-strand112-11543
α-helix116-1172
α-helix118-12912
β-strand134-13964
β-strand142-14764
β-strand152-15544
β-strand162-16434
β-strand165-16953
β-strand176-17723
β-strand180-18123
Chains B and D: 8 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix0-1516
α-helix17-182
β-strand21-2665
β-strand29-38105
α-helix39-402
β-strand49-5575
α-helix64-652
β-strand66-6945
β-strand7516
β-strand7816
β-strand8315
β-strand8416
α-helix87-893
α-helix99-11113
α-helix121-1299
α-helix131-14616
Chain C: 8 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix341
β-strand3517
α-helix361
β-strand4217
α-helix431
β-strand46-4838
β-strand54-5638
α-helix57-648
α-helix75-784
β-strand8718
α-helix90-989
β-strand103-10979
β-strand112-11549
α-helix116-1172
α-helix118-12912
β-strand134-139610
β-strand142-147610
β-strand152-155410
β-strand163-164210
β-strand165-16959
β-strand176-17729
β-strand180-18129

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase RNF146A, Cprotein155Mus musculusQ9CZW6 (AlphaFold model)
Ubiquitin-conjugating enzyme E2 D1B, Dprotein154Homo sapiensP51668 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>4QPL_1 E3 ubiquitin-protein ligase RNF146 (chains A, C)
GSLTVPECAICLQTCVHPVSLPCKHVFCYLCVKGASWLGKRCALCRQEIPEDFLDKPTLL
SPEELKAASRGNGEYAWYYEGRNGWWQYDERTSRELEDAFSKGKKNTEMLIAGFLYVADL
ENMVQYRRNEHGRRRKIKRDIIDIPKKGVAGLRLD
Sequence of entity 2 (B, D), FASTA
>4QPL_2 Ubiquitin-conjugating enzyme E2 D1 (chains B, D)
HHHHHHAMALKRIQKELSDLQRDPPAHCSAGPVGDDLFHWQATIMGPPDSAYQGGVFFLT
VHFPTDYPFKPPKIAFTTKIYHPNINSNGSICLDILRSQWSPALTVSKVLLSICSLLCDP
NPDDPLVPDIAQIYKSDKEKYNRHAREWTQKYAM

Ligands and cofactors

IDNameFormulaCopies
V3L2'-O-(5-O-phosphono-alpha-D-ribofuranosyl)adenosine 5'-(dihydrogen phosphate)C15 H23 N5 O14 P22
ZNZinc ionZn4

Primary citation

Allosteric activation of the RNF146 ubiquitin ligase by a poly(ADP-ribosyl)ation signal. DaRosa, P.A., Wang, Z., Jiang, X. et al. Nature (2015) 517:223-226. DOI 10.1038/nature13826 · PubMed

Other PDB entries of the same protein (UniProt Q9CZW6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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