Human procaspase-7/caspase-7 heterodimer bound to Ac-DEVD-CMK. Determined by X-ray diffraction at 1.65 Å resolution. Released 8 May 2013.
Explore 4JR2 in 3D Show helices and sheets RCSB PDB PDBe
4JR2 contains 20 α-helices and 38 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 |
|---|---|---|---|
| β-strand | 59 | 1 | 1 |
| β-strand | 66 | 1 | 2 |
| β-strand | 68-74 | 7 | 3 |
| α-helix | 80-82 | 3 | |
| α-helix | 84-86 | 3 | |
| α-helix | 90-104 | 15 | |
| β-strand | 106-112 | 7 | 3 |
| α-helix | 116-127 | 12 | |
| β-strand | 134 | 1 | 2 |
| β-strand | 137-142 | 6 | 3 |
| β-strand | 145-146 | 2 | 4 |
| β-strand | 149-152 | 4 | 4 |
| β-strand | 155-158 | 4 | 4 |
| α-helix | 159-163 | 5 | |
| α-helix | 164-166 | 3 | |
| α-helix | 172-174 | 3 | |
| β-strand | 179-184 | 6 | 3 |
| β-strand | 213 | 1 | 5 |
| β-strand | 219-223 | 5 | 3 |
| β-strand | 232-234 | 3 | 6 |
| β-strand | 238-239 | 2 | 6 |
| α-helix | 240-252 | 13 | |
| α-helix | 258-272 | 15 | |
| α-helix | 280-282 | 3 | |
| β-strand | 290-293 | 4 | 3 |
| β-strand | 298 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 59 | 1 | 7 |
| β-strand | 66-74 | 9 | 3 |
| α-helix | 80-82 | 3 | |
| α-helix | 84-86 | 3 | |
| α-helix | 90-104 | 15 | |
| β-strand | 106-112 | 7 | 3 |
| α-helix | 116-128 | 13 | |
| β-strand | 134-142 | 9 | 3 |
| β-strand | 145-146 | 2 | 8 |
| β-strand | 149-152 | 4 | 8 |
| β-strand | 155-158 | 4 | 8 |
| α-helix | 159-163 | 5 | |
| α-helix | 164-166 | 3 | |
| α-helix | 172-174 | 3 | |
| β-strand | 179-184 | 6 | 3 |
| β-strand | 190 | 1 | 9 |
| β-strand | 192 | 1 | 10 |
| β-strand | 195 | 1 | 5 |
| β-strand | 219-223 | 5 | 3 |
| β-strand | 229 | 1 | 9 |
| β-strand | 232-234 | 3 | 11 |
| β-strand | 238-239 | 2 | 11 |
| α-helix | 240-252 | 13 | |
| β-strand | 257 | 1 | 12 |
| α-helix | 258-272 | 15 | |
| α-helix | 280-282 | 3 | |
| β-strand | 286 | 1 | 10 |
| β-strand | 290-293 | 4 | 3 |
| β-strand | 298 | 1 | 7 |
| β-strand | 300 | 1 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Procaspase-7 | A, B | protein | 250 | Homo sapiens | P55210 (AlphaFold model) |
| Ac-devd-cmk | C, D | protein | 6 |
>4JR2_1 Procaspase-7 (chains A, B) SNATYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYND CSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGDRCKT LLEKPKLFFIQACRGTELDDGIQAASGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWR SPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVS MLTKELYFSQ
>4JR2_2 Ac-DEVD-CMK (chains C, D) XDEVDX
Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 activation. Thomsen, N.D., Koerber, J.T., Wells, J.A. Proc Natl Acad Sci U S A (2013) 110:8477-8482. DOI 10.1073/pnas.1306759110 · PubMed
Other PDB entries of the same protein (UniProt P55210 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4JR2 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.