Crystal structure of a complex between UBC9, SUMO-1, RANGAP1 and NUP358/RANBP2. Determined by X-ray diffraction at 3.01 Å resolution. Released 7 Jun 2005.
Explore 1Z5S in 3D Show helices and sheets RCSB PDB PDBe
1Z5S contains 21 α-helices and 13 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-18 | 14 | |
| β-strand | 25-30 | 6 | 1 |
| β-strand | 36-46 | 11 | 1 |
| β-strand | 57-63 | 7 | 1 |
| α-helix | 72-73 | 2 | |
| β-strand | 74-77 | 4 | 1 |
| β-strand | 86 | 1 | 2 |
| β-strand | 91 | 1 | 1 |
| β-strand | 92 | 1 | 2 |
| α-helix | 93 | 1 | |
| α-helix | 95-97 | 3 | |
| α-helix | 109-121 | 13 | |
| α-helix | 131-139 | 9 | |
| α-helix | 141-153 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22-27 | 6 | 3 |
| β-strand | 33-38 | 6 | 3 |
| α-helix | 44-53 | 10 | |
| β-strand | 64-66 | 3 | 3 |
| β-strand | 69-70 | 2 | 3 |
| α-helix | 77-80 | 4 | |
| β-strand | 87-90 | 4 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 433-439 | 7 | |
| α-helix | 447-453 | 7 | |
| α-helix | 457-460 | 4 | |
| α-helix | 466-477 | 12 | |
| α-helix | 485-501 | 17 | |
| α-helix | 509-519 | 11 | |
| α-helix | 536-545 | 10 | |
| α-helix | 556-564 | 9 | |
| α-helix | 569-571 | 3 | |
| α-helix | 574-586 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2632-2637 | 6 | 3 |
| α-helix | 2642-2650 | 9 | |
| α-helix | 2677-2683 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2 I | A | protein | 158 | Homo sapiens | P63279 (AlphaFold model) |
| Ubiquitin-like protein SMT3C | B | protein | 82 | Homo sapiens | P63165 (AlphaFold model) |
| Ran GTPase-activating protein 1 | C | protein | 172 | Homo sapiens | P46060 (AlphaFold model) |
| Ran-binding protein 2 | D | protein | 83 | Homo sapiens | P49792 |
>1Z5S_1 Ubiquitin-conjugating enzyme E2 I (chains A) MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKL RMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELL NEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS
>1Z5S_2 Ubiquitin-like protein SMT3C (chains B) MGEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNH TPKELGMEEEDVIEVYQEQTGG
>1Z5S_3 Ran GTPase-activating protein 1 (chains C) SLNTGEPAPVLSSPPPADVSTFLAFPSPEKLLRLGPKSSVLIAQQTDTSDPEKVVSAFLK VSSVFKDEATVRMAVQDAVDALMQKAFNSSSFNSNTFLTRLLVHMGLLKSEDKVKAIANL YGPLMALNHMVQQDYFPKALAPLLLAFVTKPNSALESCSFARHSLLQTLYKV
>1Z5S_4 Ran-binding protein 2 (chains D) SLDVLIVYELTPTAEQKALATKLKLPPTFFCYKNRPDYVSEEEEDDEDFETAVKKLNGKL YLDGSEKCRPLEENTADNEKECI
Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Reverter, D., Lima, C.D. Nature (2005) 435:687-692. DOI 10.1038/nature03588 · PubMed
Other PDB entries of the same protein (UniProt P63279 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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