Structural Basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin conjugating enzyme Ubc9 and RanGAP1. Determined by X-ray diffraction at 2.5 Å resolution. Released 13 Feb 2002.
Explore 1KPS in 3D Show helices and sheets RCSB PDB PDBe
1KPS contains 34 α-helices and 18 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 | 47 | 1 | 2 |
| α-helix | 48 | 1 | |
| β-strand | 54 | 1 | 2 |
| β-strand | 57-63 | 7 | 1 |
| β-strand | 74-77 | 4 | 1 |
| β-strand | 86 | 1 | 3 |
| β-strand | 91 | 1 | 1 |
| β-strand | 92 | 1 | 3 |
| α-helix | 95-97 | 3 | |
| α-helix | 109-121 | 13 | |
| α-helix | 131-139 | 9 | |
| α-helix | 141-154 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 436-441 | 6 | |
| α-helix | 445-450 | 6 | |
| α-helix | 455-461 | 7 | |
| α-helix | 468-480 | 13 | |
| α-helix | 486-505 | 20 | |
| α-helix | 511-521 | 11 | |
| α-helix | 538-549 | 12 | |
| α-helix | 555-557 | 3 | |
| α-helix | 558-565 | 8 | |
| α-helix | 577-588 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-18 | 14 | |
| β-strand | 25-30 | 6 | 4 |
| β-strand | 36-46 | 11 | 4 |
| β-strand | 47 | 1 | 5 |
| α-helix | 48 | 1 | |
| β-strand | 54 | 1 | 5 |
| β-strand | 57-63 | 7 | 4 |
| β-strand | 74-77 | 4 | 4 |
| α-helix | 80-81 | 2 | |
| β-strand | 86 | 1 | 6 |
| β-strand | 91 | 1 | 4 |
| β-strand | 92 | 1 | 6 |
| α-helix | 95-97 | 3 | |
| α-helix | 109-121 | 13 | |
| α-helix | 131-139 | 9 | |
| α-helix | 141-154 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 436-441 | 6 | |
| α-helix | 445-449 | 5 | |
| α-helix | 455-462 | 8 | |
| α-helix | 468-480 | 13 | |
| α-helix | 486-505 | 20 | |
| α-helix | 511-521 | 11 | |
| α-helix | 532-534 | 3 | |
| α-helix | 538-549 | 12 | |
| α-helix | 555-557 | 3 | |
| α-helix | 558-565 | 8 | |
| α-helix | 577-588 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-like protein SUMO-1 conjugating enzyme | A, C | protein | 159 | Homo sapiens | P63279 (AlphaFold model) |
| Ran-GTPase activating protein 1 | B, D | protein | 171 | Mus musculus | P46061 (AlphaFold model) |
>1KPS_1 Ubiquitin-like protein SUMO-1 conjugating enzyme (chains A, C) SMSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFK LRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQEL LNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS
>1KPS_2 Ran-GTPase activating protein 1 (chains B, D) SNSGEPAPVLSSPTPTDLSTFLSFPSPEKLLRLGPKVSVLIVQQTDTSDPEKVVSAFLKV ASVFRDDASVKTAVLDAIDALMKKAFSCSSFNSNTFLTRLLIHMGLLKSEDKIKAIPSLH GPLMVLNHVVRQDYFPKALAPLLLAFVTKPNGALETCSFARHNLLQTLYNI
Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Bernier-Villamor, V., Sampson, D.A., Matunis, M.J. et al. Cell (2002) 108:345-356. DOI 10.1016/S0092-8674(02)00630-X · 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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