4V3K: RNF38-UbcH5B-UB complex

RNF38-UbcH5B-UB complex. Determined by X-ray diffraction at 2.04 Å resolution. Released 8 Apr 2015.

Method
X-ray diffraction
Resolution
2.04 Å
Organism
HOMO SAPIENS
Chains
6
Atoms
5,105
Mol. weight
70.34 kDa
Ligands
ZN
Released
8 Apr 2015

Explore 4V3K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4V3K contains 29 α-helices and 48 β-strands across 6 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: 8 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix3-1513
α-helix17-182
β-strand21-2441
β-strand32-3871
α-helix39-402
β-strand49-5571
α-helix64-652
β-strand66-6941
β-strand7512
β-strand7812
β-strand8311
β-strand8412
β-strand8613
α-helix87-893
α-helix99-11113
α-helix121-1299
α-helix131-14515
Chains B and E: 4 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand1-664
β-strand12-1764
β-strand2215
α-helix23-3412
α-helix38-403
β-strand41-4554
β-strand48-4924
α-helix50-512
β-strand5515
α-helix57-593
β-strand66-7164
β-strand7513
Chains C and F: 3 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix391-3955
β-strand398-40036
β-strand412-41327
β-strand418-41927
α-helix4241
β-strand425-42846
β-strand434-43636
α-helix437-44610
β-strand44918
β-strand45618
Chain D: 7 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix3-1513
β-strand21-2559
β-strand32-3879
α-helix39-402
β-strand49-5579
α-helix64-652
β-strand66-6949
β-strand75110
β-strand78110
β-strand8319
β-strand84110
β-strand86111
α-helix87-893
α-helix99-11012
α-helix121-1299
α-helix131-14515

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-conjugating enzyme E2 D2A, Dprotein146HOMO SAPIENSP62837 (AlphaFold model)
Polyubiquitin-CB, Eprotein81HOMO SAPIENSP0CG48 (AlphaFold model)
E3 ubiquitin-protein ligase RNF38C, Fprotein79HOMO SAPIENSQ9H0F5 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>4V3K_1 UBIQUITIN-CONJUGATING ENZYME E2 D2 (chains A, D)
ALKRIHKELNDLARDPPAQCRAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYP
FKPPKVAFTTRIYHPNINSNGSIKLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVP
EIARIYKTDREKYNRIAREWTQKYAM
Sequence of entity 2 (B, E), FASTA
>4V3K_2 POLYUBIQUITIN-C (chains B, E)
GSGGSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRT
LSDYNIQKESTLHLVLRLRGG
Sequence of entity 3 (C, F), FASTA
>4V3K_3 E3 UBIQUITIN-PROTEIN LIGASE RNF38 (chains C, F)
GSTKADIEQLPSYRFNPNNHQSEQTLCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKA
NRTCPICRADASEVHRDSE

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

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

Primary citation

Activation of a Primed Ring E3-E2-Ubiquitin Complex by Non-Covalent Ubiquitin. Buetow, L., Gabrielsen, M., Anthony, N.G. et al. Mol Cell (2015) 58:297. DOI 10.1016/J.MOLCEL.2015.02.017 · PubMed

Other PDB entries of the same protein (UniProt P62837 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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