Design and optimization of new piperidines as renin inhibitors. Determined by X-ray diffraction at 2.17 Å resolution. Released 3 Nov 2010.
Explore 3OAD in 3D Show helices and sheets RCSB PDB PDBe
3OAD contains 30 α-helices and 64 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 | 6 | 1 | 1 |
| β-strand | 8-15 | 8 | 2 |
| β-strand | 19-26 | 8 | 2 |
| β-strand | 31-38 | 8 | 2 |
| β-strand | 44-47 | 4 | 2 |
| β-strand | 48 | 1 | 3 |
| α-helix | 56-59 | 4 | |
| β-strand | 64 | 1 | 3 |
| α-helix | 66-68 | 3 | |
| β-strand | 73-83 | 11 | 2 |
| β-strand | 86-99 | 14 | 2 |
| β-strand | 102-113 | 12 | 2 |
| α-helix | 116-119 | 4 | |
| β-strand | 126-129 | 4 | 2 |
| α-helix | 133-135 | 3 | |
| α-helix | 137-139 | 3 | |
| α-helix | 140-142 | 3 | |
| α-helix | 143-148 | 6 | |
| β-strand | 153 | 1 | 1 |
| β-strand | 157-162 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 174-178 | 5 | 2 |
| α-helix | 183-185 | 3 | |
| β-strand | 186-194 | 9 | 2 |
| β-strand | 202-205 | 4 | 4 |
| β-strand | 208-210 | 3 | 5 |
| β-strand | 213-216 | 4 | 5 |
| β-strand | 221-225 | 5 | 4 |
| β-strand | 232-234 | 3 | 4 |
| α-helix | 236-246 | 11 | |
| α-helix | 248 | 1 | |
| β-strand | 249-250 | 2 | 6 |
| β-strand | 255-258 | 4 | 6 |
| α-helix | 259-264 | 6 | |
| α-helix | 265-267 | 3 | |
| β-strand | 268-272 | 5 | 5 |
| β-strand | 275-279 | 5 | 5 |
| α-helix | 281-284 | 4 | |
| β-strand | 285 | 1 | 7 |
| β-strand | 295-297 | 3 | 6 |
| β-strand | 298 | 1 | 7 |
| β-strand | 300-302 | 3 | 4 |
| α-helix | 305-306 | 2 | |
| β-strand | 313-315 | 3 | 4 |
| α-helix | 317-320 | 4 | |
| β-strand | 323-328 | 6 | 2 |
| β-strand | 333-339 | 7 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6 | 1 | 8 |
| β-strand | 8-12 | 5 | 9 |
| β-strand | 13-15 | 3 | 10 |
| β-strand | 19-21 | 3 | 10 |
| β-strand | 22-26 | 5 | 11 |
| β-strand | 31-38 | 8 | 11 |
| β-strand | 44-47 | 4 | 11 |
| β-strand | 48 | 1 | 12 |
| α-helix | 56-59 | 4 | |
| β-strand | 64 | 1 | 12 |
| α-helix | 66-68 | 3 | |
| β-strand | 73-83 | 11 | 11 |
| β-strand | 86-99 | 14 | 11 |
| β-strand | 102-113 | 12 | 11 |
| α-helix | 119-121 | 3 | |
| β-strand | 126-129 | 4 | 11 |
| α-helix | 133-135 | 3 | |
| α-helix | 137-139 | 3 | |
| α-helix | 143-149 | 7 | |
| β-strand | 153 | 1 | 8 |
| β-strand | 157-162 | 6 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 174-178 | 5 | 9 |
| α-helix | 183-185 | 3 | |
| β-strand | 186-194 | 9 | 9 |
| β-strand | 195 | 1 | 13 |
| β-strand | 202-210 | 9 | 13 |
| β-strand | 213-216 | 4 | 13 |
| β-strand | 221-225 | 5 | 13 |
| β-strand | 232-234 | 3 | 13 |
| α-helix | 236-246 | 11 | |
| β-strand | 249-250 | 2 | 14 |
| β-strand | 255-258 | 4 | 14 |
| α-helix | 262-264 | 3 | |
| α-helix | 266-267 | 2 | |
| β-strand | 268-272 | 5 | 13 |
| β-strand | 276-279 | 4 | 13 |
| α-helix | 280 | 1 | |
| α-helix | 281-284 | 4 | |
| β-strand | 285 | 1 | 15 |
| β-strand | 295-297 | 3 | 14 |
| β-strand | 298 | 1 | 15 |
| β-strand | 300-302 | 3 | 13 |
| α-helix | 305-306 | 2 | |
| β-strand | 313-315 | 3 | 13 |
| α-helix | 317-322 | 6 | |
| β-strand | 323-328 | 6 | 9 |
| β-strand | 333-339 | 7 | 9 |
| α-helix | 340 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Renin | A, C | protein | 166 | Homo sapiens | P00797 (AlphaFold model) |
| Renin | B, D | protein | 176 | Homo sapiens | P00797 (AlphaFold model) |
>3OAD_1 Renin (chains A, C) LTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVY HKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFM LAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDS
>3OAD_2 Renin (chains B, D) SLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGAS YISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESY SSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALARHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| LPO | (3S,4R)-N-[2-chloro-5-(2-methoxyethyl)benzyl]-N-cyclopropyl-4-{6-[2-(2,6-dichlo… | C33 H38 Cl3 N3 O5 | 2 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Design and optimization of new piperidines as renin inhibitors. Corminboeuf, O., Bezencon, O., Grisostomi, C. et al. Bioorg Med Chem Lett (2010) 20:6286-6290. DOI 10.1016/j.bmcl.2010.08.086 · PubMed
Other PDB entries of the same protein (UniProt P00797 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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