Structure of the cIAP2 RING domain bound to UbcH5b. Determined by X-ray diffraction at 3.4 Å resolution. Released 9 Sept 2008.
Explore 3EB6 in 3D Show helices and sheets RCSB PDB PDBe
3EB6 contains 10 α-helices and 15 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 549-555 | 7 | |
| β-strand | 556 | 1 | 1 |
| β-strand | 564 | 1 | 1 |
| α-helix | 565 | 1 | |
| β-strand | 567-570 | 4 | 2 |
| β-strand | 575-577 | 3 | 2 |
| α-helix | 582-584 | 3 | |
| β-strand | 587 | 1 | 3 |
| α-helix | 593 | 1 | |
| β-strand | 594 | 1 | 3 |
| α-helix | 595 | 1 | |
| β-strand | 597-600 | 4 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-15 | 14 | |
| β-strand | 21-25 | 5 | 4 |
| β-strand | 32-37 | 6 | 4 |
| β-strand | 50-55 | 6 | 4 |
| β-strand | 66-69 | 4 | 4 |
| β-strand | 75 | 1 | 5 |
| β-strand | 78 | 1 | 5 |
| β-strand | 83 | 1 | 4 |
| β-strand | 84 | 1 | 5 |
| α-helix | 99-111 | 13 | |
| α-helix | 121-129 | 9 | |
| α-helix | 131-141 | 11 | |
| α-helix | 142-146 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Baculoviral IAP repeat-containing protein 3 | A | protein | 74 | Homo sapiens | Q13489 (AlphaFold model) |
| Ubiquitin-conjugating enzyme E2 D2 | B | protein | 149 | Xenopus laevis | P62840 (AlphaFold model) |
>3EB6_1 Baculoviral IAP repeat-containing protein 3 (chains A) LGSGTTEDVSDLPVEEQLRRLQEERTCKVCMDKEVSIVFIPCGHLVVCKDCAPSLRKCPI CRSTIKGTVRTFLS
>3EB6_2 Ubiquitin-conjugating enzyme E2 D2 (chains B) GSMALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPT DYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDP LVPEIARIYKTDREKYNRIAREWTQKYAM
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Structures of the cIAP2 RING Domain Reveal Conformational Changes Associated with Ubiquitin-conjugating Enzyme (E2) Recruitment. Mace, P.D., Linke, K., Feltham, R. et al. J Biol Chem (2008) 283:31633-31640. DOI 10.1074/jbc.M804753200 · PubMed
Other PDB entries of the same protein (UniProt Q13489 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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