Human angiotensin-1 converting enzyme C-domain in complex with quinaprilat. Determined by X-ray diffraction at 1.5 Å resolution. Released 3 Sept 2025.
Explore 9QAP in 3D Show helices and sheets RCSB PDB PDBe
9QAP contains 39 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 | 75-101 | 27 | |
| 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 | 194-196 | 3 | |
| α-helix | 197-210 | 14 | |
| α-helix | 216-221 | 6 | |
| α-helix | 222-224 | 3 | |
| 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 | 298-303 | 6 | |
| α-helix | 308-321 | 14 | |
| α-helix | 325-328 | 4 | |
| α-helix | 329-334 | 6 | |
| β-strand | 336 | 1 | 3 |
| β-strand | 351-354 | 4 | 3 |
| β-strand | 361-364 | 4 | 3 |
| α-helix | 371-389 | 19 | |
| α-helix | 395-397 | 3 | |
| α-helix | 403-417 | 15 | |
| α-helix | 420-425 | 6 | |
| α-helix | 432-446 | 15 | |
| α-helix | 449-464 | 16 | |
| α-helix | 470-472 | 3 | |
| α-helix | 473-480 | 8 | |
| α-helix | 481-485 | 5 | |
| β-strand | 487-488 | 2 | 2 |
| α-helix | 499-502 | 4 | |
| α-helix | 513-532 | 20 | |
| α-helix | 539-541 | 3 | |
| α-helix | 548-558 | 11 | |
| α-helix | 566-574 | 9 | |
| α-helix | 582-601 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensin-converting enzyme, soluble form | A | protein | 578 | Homo sapiens | P12821 (AlphaFold model) |
>9QAP_1 Angiotensin-converting enzyme, soluble form (chains A) DEAEASKFVEEYDRTSQVVWNEYAGANWNYNTNITTETSKILLQKNMQIAQHTLKYGTQA RKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPQGSCL QLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDAGDS WRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMW AQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWQKS MLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPV ALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKMALDKIAFIP FSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPSSVP YIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQ LITGQPQMSASAMLSYFKPLLDWLRTENELHGEKLGWP
Water and common crystallization additives (CL, PEG, EDO, GOL, IMD, NA) 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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