Human angiotensin-1 converting enzyme C-domain in complex with ramiprilat. Determined by X-ray diffraction at 1.5 Å resolution. Released 3 Sept 2025.
Explore 9QAN in 3D Show helices and sheets RCSB PDB PDBe
9QAN contains 37 α-helices and 7 β-strands across 1 chain. 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 | 41-70 | 30 | |
| α-helix | 75-100 | 26 | |
| α-helix | 104-106 | 3 | |
| α-helix | 110-119 | 10 | |
| α-helix | 123-126 | 4 | |
| α-helix | 129-148 | 20 | |
| β-strand | 150-152 | 3 | 1 |
| β-strand | 158-160 | 3 | 1 |
| α-helix | 161-165 | 5 | |
| α-helix | 166-171 | 6 | |
| α-helix | 175-185 | 11 | |
| α-helix | 186-190 | 5 | |
| α-helix | 191-193 | 3 | |
| α-helix | 197-210 | 14 | |
| α-helix | 216-222 | 7 | |
| α-helix | 229-239 | 11 | |
| α-helix | 241-259 | 19 | |
| α-helix | 269 | 1 | |
| β-strand | 270-271 | 2 | 2 |
| α-helix | 284-286 | 3 | |
| α-helix | 287-290 | 4 | |
| α-helix | 301-307 | 7 | |
| α-helix | 312-325 | 14 | |
| α-helix | 329-332 | 4 | |
| α-helix | 333-338 | 6 | |
| β-strand | 340 | 1 | 3 |
| β-strand | 355-358 | 4 | 3 |
| β-strand | 365-368 | 4 | 3 |
| α-helix | 375-393 | 19 | |
| α-helix | 399-401 | 3 | |
| α-helix | 407-421 | 15 | |
| α-helix | 424-429 | 6 | |
| α-helix | 440-454 | 15 | |
| α-helix | 457-472 | 16 | |
| α-helix | 478-480 | 3 | |
| α-helix | 481-488 | 8 | |
| α-helix | 489-493 | 5 | |
| β-strand | 495-496 | 2 | 2 |
| α-helix | 507-510 | 4 | |
| α-helix | 521-540 | 20 | |
| α-helix | 547-549 | 3 | |
| α-helix | 556-566 | 11 | |
| α-helix | 574-582 | 9 | |
| α-helix | 590-610 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensin-converting enzyme | A | protein | 597 | Homo sapiens | P12821 (AlphaFold model) |
>9QAN_1 Angiotensin-converting enzyme (chains A) LVTDEAEASKFVEEYDRTSQVVWNEYAGANWNYNTNITTETSKILLQKNMQIAQHTLKYG TQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPQG SCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDA GDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLG NMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFW QKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKD LPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKMALDKIA FIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPS SVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPE AMQLITGQPQMSASAMLSYFKPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLP
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
| X92 | Ramiprilat | C21 H28 N2 O5 | 1 |
| BO3 | Boric acid | B H3 O3 | 2 |
| ZN | Zinc ion | Zn | 1 |
Water and common crystallization additives (IMD, EDO, PGE, CL) are not listed.
Molecular basis of domain-specific angiotensin I-converting enzyme inhibition by the antihypertensive drugs enalaprilat, ramiprilat, trandolaprilat, quinaprilat and perindoprilat. Gregory, K.S., Ramasamy, V., Sturrock, E.D. et al. FEBS J (2026) 293:475-491. DOI 10.1111/febs.70232 · PubMed
Other PDB entries of the same protein (UniProt P12821 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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