Crystal structure of human testis angiotensin-I converting enzyme mutant D465T. Determined by X-ray diffraction at 1.8 Å resolution. Released 11 Dec 2013.
Explore 4C2O in 3D Show helices and sheets RCSB PDB PDBe
4C2O contains 36 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 | 75-99 | 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 | 197-210 | 14 | |
| α-helix | 216-222 | 7 | |
| α-helix | 229-239 | 11 | |
| α-helix | 241-259 | 19 | |
| α-helix | 261-263 | 3 | |
| 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 | 407-421 | 15 | |
| α-helix | 424-429 | 6 | |
| α-helix | 440-473 | 34 | |
| 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 | 589 | HOMO SAPIENS | P12821 (AlphaFold model) |
>4C2O_1 ANGIOTENSIN-CONVERTING ENZYME (chains A) LVTDEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYG TQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHPNG SCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDA GDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLG NMWAQTWSNIYDLVVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFW NKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKD LPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGSDEHDINFLMKMALDKIA FIPFSYLVTQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHIPS SVPYIRYFVSFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPE AMQLITGQPNMSASAMLSYFKPLLDWLRTENELHGEKLGWPQYNWTPNS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
| MLA | Malonic acid | C3 H4 O4 | 1 |
| PE4 | 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-etha… | C16 H34 O8 | 1 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
Water and common crystallization additives (SO4, ACT, CL) are not listed.
Molecular and Thermodynamic Mechanisms of the Chloride Dependent Human Angiotensin-I Converting Enzyme (Ace). Yates, C.J., Masuyer, G., Schwager, S.L.U. et al. J Biol Chem (2014) 289:1798. DOI 10.1074/JBC.M113.512335 · 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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