Structure-based design of 4-hydroxy-3,5-substituted piperidines as direct renin inhibitors. Determined by X-ray diffraction at 2.09 Å resolution. Released 6 Aug 2014.
Explore 4Q1N in 3D Show helices and sheets RCSB PDB PDBe
4Q1N contains 28 α-helices and 64 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 |
|---|---|---|---|
| β-strand | 0 | 1 | 1 |
| β-strand | 2-6 | 5 | 2 |
| β-strand | 7-9 | 3 | 3 |
| β-strand | 13-20 | 8 | 3 |
| β-strand | 25-32 | 8 | 3 |
| β-strand | 38-41 | 4 | 3 |
| β-strand | 42 | 1 | 4 |
| α-helix | 48-51 | 4 | |
| β-strand | 56 | 1 | 4 |
| α-helix | 58-60 | 3 | |
| β-strand | 65-75 | 11 | 3 |
| β-strand | 78-91 | 14 | 3 |
| β-strand | 94-106 | 12 | 3 |
| α-helix | 109-112 | 4 | |
| β-strand | 119-122 | 4 | 3 |
| α-helix | 126-128 | 3 | |
| α-helix | 130-132 | 3 | |
| α-helix | 133-135 | 3 | |
| α-helix | 136-142 | 7 | |
| β-strand | 146 | 1 | 1 |
| β-strand | 150-155 | 6 | 2 |
| β-strand | 163-167 | 5 | 2 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-183 | 9 | 2 |
| β-strand | 191-194 | 4 | 5 |
| β-strand | 196-199 | 4 | 6 |
| β-strand | 202-205 | 4 | 6 |
| β-strand | 210-214 | 5 | 5 |
| β-strand | 221-223 | 3 | 5 |
| α-helix | 225-235 | 11 | |
| β-strand | 238-239 | 2 | 7 |
| β-strand | 245-248 | 4 | 7 |
| α-helix | 249-254 | 6 | |
| α-helix | 255-257 | 3 | |
| β-strand | 258-262 | 5 | 6 |
| β-strand | 265-269 | 5 | 6 |
| α-helix | 271-274 | 4 | |
| β-strand | 275 | 1 | 8 |
| β-strand | 281D-283 | 3 | 7 |
| β-strand | 284 | 1 | 8 |
| β-strand | 286-288 | 3 | 5 |
| α-helix | 291-292 | 2 | |
| β-strand | 299-301 | 3 | 5 |
| α-helix | 303-308 | 6 | |
| β-strand | 309-314 | 6 | 2 |
| β-strand | 319-325 | 7 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 0 | 1 | 9 |
| β-strand | 2-6 | 5 | 10 |
| β-strand | 7-9 | 3 | 11 |
| β-strand | 13-20 | 8 | 11 |
| β-strand | 25-32 | 8 | 11 |
| β-strand | 38-41 | 4 | 11 |
| β-strand | 42 | 1 | 12 |
| α-helix | 49-52 | 4 | |
| β-strand | 56 | 1 | 12 |
| α-helix | 58-60 | 3 | |
| β-strand | 65-75 | 11 | 11 |
| β-strand | 78-91 | 14 | 11 |
| β-strand | 94-106 | 12 | 11 |
| α-helix | 109-112 | 4 | |
| β-strand | 119-122 | 4 | 11 |
| α-helix | 126-128 | 3 | |
| α-helix | 130-132 | 3 | |
| α-helix | 133-135 | 3 | |
| α-helix | 136-142 | 7 | |
| β-strand | 146 | 1 | 9 |
| β-strand | 150-155 | 6 | 10 |
| β-strand | 163-167 | 5 | 10 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-183 | 9 | 10 |
| β-strand | 191-194 | 4 | 13 |
| β-strand | 196-199 | 4 | 14 |
| β-strand | 202-205 | 4 | 14 |
| β-strand | 210-214 | 5 | 13 |
| β-strand | 221-223 | 3 | 13 |
| α-helix | 225-235 | 11 | |
| β-strand | 238-239 | 2 | 15 |
| β-strand | 245-248 | 4 | 15 |
| α-helix | 249-254 | 6 | |
| α-helix | 256-257 | 2 | |
| β-strand | 258-262 | 5 | 14 |
| β-strand | 265-269 | 5 | 14 |
| α-helix | 271-274 | 4 | |
| β-strand | 275 | 1 | 16 |
| β-strand | 281D-283 | 3 | 15 |
| β-strand | 284 | 1 | 16 |
| β-strand | 286-288 | 3 | 13 |
| α-helix | 291-292 | 2 | |
| β-strand | 299-301 | 3 | 13 |
| α-helix | 303-308 | 6 | |
| β-strand | 309-314 | 6 | 10 |
| β-strand | 319-325 | 7 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Renin | A, B | protein | 340 | Homo sapiens | P00797 (AlphaFold model) |
>4Q1N_1 Renin (chains A, B) LTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVY HKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFM LAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDSENSQSLGGQIVLGG SDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIE KLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAI HAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
| ID | Name | Formula | Copies |
|---|---|---|---|
| 2Y9 | (3S,4R,5R)-N-cyclopropyl-N'-[(2R)-1-ethoxy-4-methylpentan-2-yl]-4-hydroxy-N-[5-… | C26 H42 N4 O4 | 2 |
| PO4 | Phosphate ion | O4 P | 1 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Water and common crystallization additives (DMS) are not listed.
Structure-based design of substituted piperidines as a new class of highly efficacious oral direct Renin inhibitors. Ehara, T., Irie, O., Kosaka, T. et al. ACS Med Chem Lett (2014) 5:787-792. DOI 10.1021/ml500137b · 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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