DUBS Parachlamydia sp. PcJOS orthorhombic crystal form. Determined by X-ray diffraction at 2.18 Å resolution. Released 23 Apr 2025.
Explore 9FPA in 3D Show helices and sheets RCSB PDB PDBe
9FPA contains 32 α-helices and 40 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 98-100 | 3 | |
| α-helix | 103-107 | 5 | |
| α-helix | 111-121 | 11 | |
| β-strand | 123 | 1 | 10 |
| β-strand | 125 | 1 | 11 |
| β-strand | 128 | 1 | 11 |
| α-helix | 134-138 | 5 | |
| α-helix | 154-156 | 3 | |
| α-helix | 162-171 | 10 | |
| α-helix | 178-193 | 16 | |
| α-helix | 197-205 | 9 | |
| β-strand | 212 | 1 | 3 |
| α-helix | 214-225 | 12 | |
| β-strand | 229-233 | 5 | 12 |
| α-helix | 234-236 | 3 | |
| α-helix | 244-252 | 9 | |
| β-strand | 257-262 | 6 | 12 |
| β-strand | 268 | 1 | 10 |
| β-strand | 280 | 1 | 10 |
| β-strand | 284-290 | 7 | 12 |
| β-strand | 296-299 | 4 | 12 |
| β-strand | 307-308 | 2 | 12 |
| α-helix | 311-313 | 3 | |
| β-strand | 319-323 | 5 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-7 | 6 | 1 |
| β-strand | 12-16 | 5 | 1 |
| β-strand | 22 | 1 | 2 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 1 |
| β-strand | 48-49 | 2 | 1 |
| β-strand | 55 | 1 | 2 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-71 | 6 | 1 |
| β-strand | 73 | 1 | 3 |
| β-strand | 77-82 | 6 | 4 |
| β-strand | 88-93 | 6 | 4 |
| β-strand | 98 | 1 | 5 |
| α-helix | 99-110 | 12 | |
| α-helix | 114-116 | 3 | |
| β-strand | 117-121 | 5 | 4 |
| β-strand | 124-125 | 2 | 4 |
| α-helix | 126-127 | 2 | |
| β-strand | 131 | 1 | 5 |
| α-helix | 133-135 | 3 | |
| β-strand | 142-147 | 6 | 4 |
| β-strand | 148 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 98-100 | 3 | |
| α-helix | 103-107 | 5 | |
| α-helix | 111-121 | 11 | |
| β-strand | 123 | 1 | 7 |
| α-helix | 134-138 | 5 | |
| β-strand | 141 | 1 | 8 |
| α-helix | 146-147 | 2 | |
| α-helix | 162-171 | 10 | |
| α-helix | 178-192 | 15 | |
| α-helix | 198-205 | 8 | |
| α-helix | 207-209 | 3 | |
| β-strand | 211 | 1 | 6 |
| α-helix | 214-225 | 12 | |
| β-strand | 229-233 | 5 | 9 |
| α-helix | 234-236 | 3 | |
| α-helix | 244-252 | 9 | |
| β-strand | 257-261 | 5 | 9 |
| β-strand | 268 | 1 | 7 |
| β-strand | 280 | 1 | 7 |
| β-strand | 285-290 | 6 | 9 |
| β-strand | 296-299 | 4 | 9 |
| β-strand | 307-308 | 2 | 9 |
| β-strand | 309 | 1 | 8 |
| α-helix | 311-313 | 3 | |
| β-strand | 319-323 | 5 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin | B | protein | 152 | Homo sapiens | F5H388 (AlphaFold model) |
| Peptidase C39-like domain-containing protein | A, C | protein | 255 | Parachlamydia sp. | A0A2H9SU66 (AlphaFold model) |
>9FPA_1 Ubiquitin (chains B) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLI FAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
>9FPA_2 Peptidase C39-like domain-containing protein (chains A, C) KTQPSTTQKVENTAKTLFKPDLKSPPMNPQWLTEEQIKKMSPDEQGNLIDTYAARKINAA SDLTHAQLRGMIGSTAASHIAIVNAQETGLGHAGRYAINNALQQEALSQNEFLSLTGQIF SNQLGMSLADVKNLIQNQDDFGIDTGVLAQILKQKFNQPVKESKICDLPDCALSKQQAVE NYIGKAKWVIVANIGTEVFDMPSSTHAVYPLTRGHFVALRRDADNRWWYLDSRGKNPVNI ALAIIPRTCTLIVPL
| ID | Name | Formula | Copies |
|---|---|---|---|
| CIT | Citric acid | C6 H8 O7 | 2 |
A family of bacterial Josephin-like deubiquitinases with an irreversible cleavage mode. Hermanns, T., Kolek, S., Uthoff, M. et al. Mol Cell (2025) 85:1202-1215.e5. DOI 10.1016/j.molcel.2025.02.002 · PubMed
Other PDB entries of the same protein (UniProt F5H388 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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