Caspase-7 in Complex with DARPin D7.18. Determined by X-ray diffraction at 2.26 Å resolution. Released 2 Jul 2014.
Explore 4LSZ in 3D Show helices and sheets RCSB PDB PDBe
4LSZ contains 40 α-helices and 38 β-strands across 6 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 |
|---|---|---|---|
| β-strand | 59 | 1 | 1 |
| β-strand | 66-74 | 9 | 2 |
| α-helix | 80-82 | 3 | |
| α-helix | 84-86 | 3 | |
| α-helix | 90-104 | 15 | |
| β-strand | 106-112 | 7 | 2 |
| α-helix | 116-127 | 12 | |
| β-strand | 134-142 | 9 | 2 |
| β-strand | 145-146 | 2 | 3 |
| β-strand | 149-152 | 4 | 3 |
| β-strand | 155-158 | 4 | 3 |
| α-helix | 159-163 | 5 | |
| α-helix | 164-166 | 3 | |
| α-helix | 172-174 | 3 | |
| β-strand | 179-184 | 6 | 2 |
| β-strand | 190 | 1 | 4 |
| β-strand | 192 | 1 | 5 |
| β-strand | 195-196 | 2 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 212-213 | 2 | 7 |
| β-strand | 219-223 | 5 | 2 |
| β-strand | 229 | 1 | 4 |
| β-strand | 233-234 | 2 | 8 |
| β-strand | 238-239 | 2 | 8 |
| α-helix | 240-252 | 13 | |
| α-helix | 258-272 | 15 | |
| α-helix | 280-282 | 3 | |
| β-strand | 286 | 1 | 5 |
| β-strand | 290-293 | 4 | 2 |
| β-strand | 298 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 59 | 1 | 9 |
| β-strand | 66-74 | 9 | 2 |
| α-helix | 80-82 | 3 | |
| α-helix | 90-104 | 15 | |
| β-strand | 107-112 | 6 | 2 |
| α-helix | 116-127 | 12 | |
| β-strand | 134-142 | 9 | 2 |
| β-strand | 145-146 | 2 | 10 |
| β-strand | 149-151 | 3 | 10 |
| β-strand | 156-158 | 3 | 10 |
| α-helix | 159-163 | 5 | |
| α-helix | 164-166 | 3 | |
| α-helix | 172-174 | 3 | |
| β-strand | 179-184 | 6 | 2 |
| β-strand | 190 | 1 | 11 |
| β-strand | 192 | 1 | 12 |
| β-strand | 195-196 | 2 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-24 | 12 | |
| α-helix | 27-35 | 9 | |
| α-helix | 50-56 | 7 | |
| α-helix | 60-68 | 9 | |
| α-helix | 83-90 | 8 | |
| α-helix | 93-101 | 9 | |
| α-helix | 116-122 | 7 | |
| α-helix | 126-134 | 9 | |
| α-helix | 149-155 | 7 | |
| α-helix | 159-163 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-24 | 11 | |
| α-helix | 27-35 | 9 | |
| α-helix | 50-56 | 7 | |
| α-helix | 60-68 | 9 | |
| α-helix | 83-90 | 8 | |
| α-helix | 93-101 | 9 | |
| α-helix | 116-122 | 7 | |
| α-helix | 126-134 | 9 | |
| α-helix | 141-143 | 3 | |
| α-helix | 149-155 | 7 | |
| α-helix | 159-165 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Caspase-7 subunit p20 | A, C | protein | 175 | Homo sapiens | P55210 (AlphaFold model) |
| Caspase-7 subunit p10 | B, D | protein | 105 | Homo sapiens | P55210 (AlphaFold model) |
| DARPin D7.18 | E, F | protein | 169 | synthetic construct |
>4LSZ_1 Caspase-7 subunit p20 (chains A, C) AKPDRSSFVPSLFSKKKKNVTMRSIKTTRDRVPTYQYNMNFEKLGKCIIINNKNFDKVTG MGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLS HGEENVIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQAD
>4LSZ_2 Caspase-7 subunit p10 (chains B, D) ANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVN DRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQLEHHHHHH
>4LSZ_3 DARPin D7.18 (chains E, F) MRGSHHHHHHGSDLGKKLLEAARAGQDDEVRILMANGADVNADDAWGQTPLHLAAQNGHL EIVEVLLKHDADVNATDWVGMTPLHLAADDGHLEIVEALLKYGADVNAYDQLGNTPLNLA ATDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEILQKLN
Combined inhibition of caspase 3 and caspase 7 by two highly selective DARPins slows down cellular demise. Flutsch, A., Ackermann, R., Schroeder, T. et al. Biochem J (2014) 461:279-290. DOI 10.1042/BJ20131456 · PubMed
Other PDB entries of the same protein (UniProt P55210 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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