Human angiotensin-converting enzyme in complex with BPPb. Determined by X-ray diffraction at 2.6 Å resolution. Released 17 Oct 2012.
Explore 4APJ in 3D Show helices and sheets RCSB PDB PDBe
4APJ contains 40 α-helices and 8 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 |
|---|---|---|---|
| α-helix | 41-71 | 31 | |
| α-helix | 75-99 | 25 | |
| 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 | 197-209 | 13 | |
| 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 | 301-307 | 7 | |
| α-helix | 312-325 | 14 | |
| α-helix | 328-332 | 5 | |
| 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 | 407-422 | 16 | |
| α-helix | 424-429 | 6 | |
| α-helix | 440-454 | 15 | |
| α-helix | 457-473 | 17 | |
| 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 | 556-567 | 12 | |
| α-helix | 574-582 | 9 | |
| α-helix | 590-595 | 6 | |
| α-helix | 597-610 | 14 | |
| α-helix | 612-613 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-7 | 4 | |
| β-strand | 8 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensin-converting enzyme | A | protein | 589 | HOMO SAPIENS | P12821 (AlphaFold model) |
| Bradykinin-potentiating peptide B | P | protein | 11 | GLOYDIUS BLOMHOFFI | P01021 (AlphaFold model) |
>4APJ_1 ANGIOTENSIN-CONVERTING ENZYME (chains A) LVTDEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYG TQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPNG SCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDA GDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLG NMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFW NKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKD LPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKMALDKIA FIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPS SVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPE AMQLITGQPNMSASAMLSYFKPLLDWLRTENELHGEKLGWPQYNWTPNS
>4APJ_2 BRADYKININ-POTENTIATING PEPTIDE B (chains P) QGLPPRPKIPP
| ID | Name | Formula | Copies |
|---|---|---|---|
| PE4 | 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-etha… | C16 H34 O8 | 3 |
Water and common crystallization additives (CL, SO4, ACT) are not listed.
Molecular Recognition and Regulation of Human Angiotensin-I Converting Enzyme (Ace) Activity by Natural Inhibitory Peptides. Masuyer, G., Schwager, S.L.U., Sturrock, E.D. et al. Sci Rep (2012) 2:717. DOI 10.1038/SREP00717 · 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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