Crystal structure of Burkholderia pseudomallei effector protein CHBP in complex with ubiquitin. Determined by X-ray diffraction at 2.6 Å resolution. Released 21 Nov 2012.
Explore 4HCN in 3D Show helices and sheets RCSB PDB PDBe
4HCN contains 22 α-helices and 16 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 | 81-95 | 15 | |
| α-helix | 99-105 | 7 | |
| α-helix | 114-116 | 3 | |
| α-helix | 119-132 | 14 | |
| α-helix | 136-142 | 7 | |
| α-helix | 151-152 | 2 | |
| β-strand | 154 | 1 | 1 |
| α-helix | 156-168 | 13 | |
| α-helix | 176-178 | 3 | |
| β-strand | 182 | 1 | 2 |
| α-helix | 187-191 | 5 | |
| β-strand | 199-206 | 8 | 2 |
| β-strand | 211-217 | 7 | 2 |
| β-strand | 228-230 | 3 | 2 |
| β-strand | 233 | 1 | 3 |
| α-helix | 240-241 | 2 | |
| β-strand | 242 | 1 | 3 |
| α-helix | 244-251 | 8 | |
| α-helix | 258-264 | 7 | |
| α-helix | 267-271 | 5 | |
| α-helix | 274-285 | 12 | |
| α-helix | 291-293 | 3 | |
| α-helix | 296-298 | 3 | |
| α-helix | 303-304 | 2 | |
| β-strand | 305-312 | 8 | 2 |
| α-helix | 314-325 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-7 | 6 | 4 |
| β-strand | 12-16 | 5 | 4 |
| β-strand | 22 | 1 | 5 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 42-45 | 4 | 4 |
| β-strand | 48-49 | 2 | 4 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 5 |
| α-helix | 57-59 | 3 | |
| β-strand | 65-70 | 6 | 4 |
| β-strand | 72 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Putative ATP/GTP binding protein | A | protein | 255 | Burkholderia pseudomallei | Q63KH5 (AlphaFold model) |
| Polyubiquitin | B | protein | 98 | Saccharomyces cerevisiae | P0CG63 (AlphaFold model) |
>4HCN_1 Putative ATP/GTP binding protein (chains A) SGRPLKHRVTLRKATLASLMQSLSGESSNRVMWNDRYDTLLIARDPREIKNAIEKSVTDF GGLENYKELTGGADPFALMTPVAGLSANNIFKLMTEKDVPIDPTSIEYLENTSFAEHVNT LDSHKNYVVIVNDGRLGHKFLIDLPALTQGPRTAYIIQSDLGGGALPAVRVEDWISRRGS DPVSLDELNQLLSKDFSKMPDDVQTRLLASILQIDKDPHKVDIKKLHLDGKLRFASHEYD FRQFQRNAQYVAGLG
>4HCN_2 Polyubiquitin (chains B) MGSSHHHHHHSSGENLYFQGRPMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPP DQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 1 |
Water and common crystallization additives (PEG, FMT) are not listed.
Structural mechanism of ubiquitin and NEDD8 deamidation catalyzed by bacterial effectors that induce macrophage-specific apoptosis. Yao, Q., Cui, J., Wang, J. et al. Proc Natl Acad Sci U S A (2012) 109:20395-20400. DOI 10.1073/pnas.1210831109 · PubMed
Other PDB entries of the same protein (UniProt Q63KH5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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