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2YHO: 
The IDOL-UBE2D complex mediates sterol-dependent degradation of the LDL receptor
Biological unit 1: dimeric
Source organism: Homo sapiens
Number of proteins:
2 (E3 UBIQUITIN-PROTEIN LIGASE MYLIP, UBIQUITIN-CO... ▼)
Protein molecule
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 E3 UBIQUITIN-PROTEIN LIGASE MYLIP
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 UBIQUITIN-CONJUGATING ENZYME E2 D1
Number of chemicals:
6 (ACETATE ION (4),ZINC ION (2) ▼)
Chemical
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ACETATE ION (4)
ZINC ION (2)
Similar Structures (491)help
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Showing 1 to 10 out of 491 selected structures help
      PDB ID Description Taxonomy▲▼ Aligned Protein▲▼ RMSD▲▼ Aligned Residues▲▼ Sequence Identity▲▼
1
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 6HPR
Crystal structure of cIAP1 RING domain bound to UbcH5B-Ub and a non-covalent Ub
Homo sapiens
 2 1.43Å 204 74%
2
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Full
 3EB6
Structure of the cIAP2 RING domain bound to UbcH5b
Xenopus laevis/Homo sapiens
 2 1.48Å 201 76%
3
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Full
 6S53
Crystal structure of TRIM21 RING domain in complex with an isopeptide-linked Ube2N~ubiquitin conjugate
Homo sapiens
 2 1.87Å 197 39%
4
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Full
 6FGA
Crystal structure of TRIM21 E3 ligase, RING domain in complex with its cognate E2 conjugating enzyme UBE2E1
Homo sapiens
 2 1.67Å 179 53%
5
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Partial
 2OXQ
Structure of the UbcH5 :CHIP U-box complex
Danio rerio
 1 0.70Å 149 93%
6
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Partial
 3TGD
Crystal structure of the human ubiquitin-conjugating enzyme (E2) UbcH5b
Homo sapiens
 1 0.94Å 149 88%
7
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Partial
 3L1Y
Crystal structure of human UBC4 E2 conjugating enzyme
Homo sapiens
 1 0.96Å 149 87%
8
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Partial
 1Z2U
The 1.1A crystallographic structure of ubiquitin-conjugating enzyme (ubc-2) from Caenorhabditis elegans: functional and evolutionary significance
Caenorhabditis elegans
 1 1.02Å 149 87%
9
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Partial
 4R8P
Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle
Others
 1 1.43Å 149 86%
10
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Partial
 3BZH
Crystal structure of human ubiquitin-conjugating enzyme E2 E1
Homo sapiens
 1 0.71Å 148 60%
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{"1":"E3 UBIQUITIN-PROTEIN LIGASE MYLIP","2":"UBIQUITIN-CONJUGATING ENZYME E2 D1"}
Citing VAST
Gibrat JF, Madej T, Bryant SH. "Surprising similarities in structure comparison.", Curr Opin Struct Biol.1996 Jun;6(3):377-85
Madej T, Lanczycki CJ, Zhang D, Thiessen PA, Geer RC, Marchler-Bauer A, Bryant SH. "MMDB and VAST+: tracking structural similarities between macromolecular complexes." Nucl. Acids Res. 2014 Jan;42(Database issue):D297-303
Thomas Madej, Aron Marchler-Bauer, Christopher Lanczycki, Dachuan Zhang, Stephen H Bryant "Biological Assembly Comparison With VAST" Methods Mol. Biol. 2020(2112):175-186
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?Original VAST
Original VAST finds structures that are similar to individual protein molecules, or individual 3D domains, in your query structure. Select a protein molecule ("chain") or 3D domain of interest from the table below to view a list of other proteins or domains that have a similar 3D shape. In contrast to VAST+, which focuses on the default biological unit, Original VAST lists all protein molecules in the asymmetric unit of the query structure.