6DJW: PDB entry 6DJW

Crystal Structure of pParkin (REP and RING2 deleted)-pUb-UbcH7 complex. Determined by X-ray diffraction at 3.8 Å resolution. Released 4 Jul 2018.

Method
X-ray diffraction
Resolution
3.8 Å
Organisms
Bactrocera dorsalis, Bos taurus, Homo sapiens
Chains
3
Atoms
4,346
Mol. weight
66.68 kDa
Ligands
ZN
Released
4 Jul 2018

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Secondary structure: helices and β-sheets

6DJW contains 19 α-helices and 41 β-strands across 3 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, 25 β-strands

ElementResiduesLengthSheet
β-strand30-3561
β-strand41-4661
β-strand5112
α-helix52-6312
β-strand70-7453
β-strand77-7823
β-strand8412
α-helix86-883
β-strand94-9631
β-strand97-10043
β-strand175-17624
β-strand18414
β-strand186-19165
β-strand20016
β-strand22216
α-helix224-2274
β-strand241-24665
β-strand259-26024
β-strand264-26637
α-helix271-2733
β-strand282-28547
β-strand293-29537
α-helix296-30510
α-helix3121
β-strand313-31538
β-strand319-32138
α-helix336-3416
α-helix344-36219
β-strand365-36629
β-strand375-37739
β-strand385110
β-strand395110
β-strand402110
Chain B: 3 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand2-659
β-strand12-1659
β-strand22111
α-helix23-3412
β-strand41-4559
β-strand48-4929
α-helix50-512
β-strand55111
α-helix57-593
β-strand66-7279
Chain C: 8 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix4-1613
β-strand22-26512
β-strand34-39612
α-helix44-463
β-strand49-50213
β-strand51-56612
α-helix61-633
α-helix65-662
β-strand67-70412
β-strand79114
β-strand84112
β-strand85114
α-helix92-943
α-helix101-11313
α-helix123-1319
α-helix134-14613
β-strand149-150213

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RBR-type E3 ubiquitin transferase,RBR-type E3 ubiquitin transferaseAprotein349Bactrocera dorsalisA0A034W4L8 (AlphaFold model)
UbiquitinBprotein74Bos taurusP62992 (AlphaFold model)
Ubiquitin-conjugating enzyme E2 L3Cprotein159Homo sapiensP68036 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6DJW_1 RBR-type E3 ubiquitin transferase,RBR-type E3 ubiquitin transferase (chains A)
GGENLYLGGSLSIYIKTNTGRTLSVNLEPQWDIKNVKEIVAPQLGLQPEEVKIIFAGKEL
SDATTIQECDLGQQSILHAIRSRPQPQRQRLQSTVMEITEEDRQRTKAHFFVHCAQCNKL
CKGKLRVRCSLCKGGAFTVHRDPECWDDVLKPRRITGHCESQEIACFDNETGDPPFTEFY
FKCGEHVSGGEKDFAAPLNLIKINIKDVPCLACTEVSETVLVFPCESKHVTCLECFEQYC
RSRLSERQFMPHPDIGYTLPCPAGCENSFIEEIHHFKLLSREEYARYQRFATEEYVLQAG
GVLCPQPGCGMGLLVEPECKKVTCQNGCGYVFCRNCLQGYHLGDCLPEG
Sequence of entity 2 (B), FASTA
>6DJW_2 Ubiquitin (chains B)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLR
Sequence of entity 3 (C), FASTA
>6DJW_3 Ubiquitin-conjugating enzyme E2 L3 (chains C)
GPLGSMAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEI
NFPAEYPFKPPKITFKTKIYHPNIDEKGQVKLPVISAENWKPATKTDQVIQSLIALVNDP
QPEHPLRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVD

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn6

Primary citation

Mechanism of parkin activation by phosphorylation. Sauve, V., Sung, G., Soya, N. et al. Nat Struct Mol Biol (2018) 25:623-630. DOI 10.1038/s41594-018-0088-7 · PubMed

Other PDB entries of the same protein (UniProt A0A034W4L8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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