Crystal structure of Angiotensin-1 converting enzyme N-domain in complex with dual ACE/NEP inhibitor AD015. Determined by X-ray diffraction at 1.7 Å resolution. Released 16 Apr 2025.
Explore 9H1B in 3D Show helices and sheets RCSB PDB PDBe
9H1B contains 72 α-helices and 14 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 | 3-5 | 3 | |
| α-helix | 14-43 | 30 | |
| α-helix | 48-76 | 29 | |
| α-helix | 80-82 | 3 | |
| α-helix | 86-95 | 10 | |
| α-helix | 99-102 | 4 | |
| α-helix | 105-124 | 20 | |
| β-strand | 126-128 | 3 | 1 |
| β-strand | 136-138 | 3 | 1 |
| α-helix | 139-143 | 5 | |
| α-helix | 144-149 | 6 | |
| α-helix | 153-187 | 35 | |
| α-helix | 194-200 | 7 | |
| α-helix | 207-237 | 31 | |
| α-helix | 247 | 1 | |
| β-strand | 248-249 | 2 | 2 |
| α-helix | 262-264 | 3 | |
| α-helix | 265-268 | 4 | |
| α-helix | 280-286 | 7 | |
| α-helix | 290-303 | 14 | |
| α-helix | 307-310 | 4 | |
| α-helix | 311-316 | 6 | |
| β-strand | 318 | 1 | 3 |
| β-strand | 333-336 | 4 | 3 |
| β-strand | 343-346 | 4 | 3 |
| α-helix | 353-372 | 20 | |
| α-helix | 377-379 | 3 | |
| α-helix | 385-399 | 15 | |
| α-helix | 402-407 | 6 | |
| α-helix | 418-432 | 15 | |
| α-helix | 435-451 | 17 | |
| α-helix | 456-458 | 3 | |
| α-helix | 459-466 | 8 | |
| α-helix | 467-471 | 5 | |
| β-strand | 473-474 | 2 | 2 |
| α-helix | 485-488 | 4 | |
| α-helix | 499-519 | 21 | |
| α-helix | 525-527 | 3 | |
| α-helix | 534-546 | 13 | |
| α-helix | 552-560 | 9 | |
| α-helix | 568-587 | 20 | |
| α-helix | 590-591 | 2 | |
| α-helix | 601-604 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-5 | 3 | |
| α-helix | 14-43 | 30 | |
| α-helix | 48-76 | 29 | |
| α-helix | 80-82 | 3 | |
| α-helix | 86-95 | 10 | |
| α-helix | 99-102 | 4 | |
| α-helix | 105-124 | 20 | |
| β-strand | 126-128 | 3 | 4 |
| β-strand | 136-138 | 3 | 4 |
| α-helix | 139-143 | 5 | |
| α-helix | 144-149 | 6 | |
| α-helix | 153-187 | 35 | |
| α-helix | 194-200 | 7 | |
| α-helix | 207-237 | 31 | |
| α-helix | 247 | 1 | |
| β-strand | 248-249 | 2 | 5 |
| α-helix | 262-264 | 3 | |
| α-helix | 265-268 | 4 | |
| α-helix | 280-286 | 7 | |
| α-helix | 290-303 | 14 | |
| α-helix | 307-310 | 4 | |
| α-helix | 311-316 | 6 | |
| β-strand | 318 | 1 | 6 |
| β-strand | 333-336 | 4 | 6 |
| β-strand | 343-346 | 4 | 6 |
| α-helix | 353-371 | 19 | |
| α-helix | 377-379 | 3 | |
| α-helix | 385-399 | 15 | |
| α-helix | 402-407 | 6 | |
| α-helix | 418-432 | 15 | |
| α-helix | 435-451 | 17 | |
| α-helix | 456-458 | 3 | |
| α-helix | 459-466 | 8 | |
| α-helix | 467-471 | 5 | |
| β-strand | 473-474 | 2 | 5 |
| α-helix | 485-488 | 4 | |
| α-helix | 499-518 | 20 | |
| α-helix | 525-527 | 3 | |
| α-helix | 534-546 | 13 | |
| α-helix | 552-560 | 9 | |
| α-helix | 568-587 | 20 | |
| α-helix | 590-591 | 2 | |
| α-helix | 601-604 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiotensin-converting enzyme, soluble form | A, B | protein | 628 | Homo sapiens | P12821 (AlphaFold model) |
>9H1B_1 Angiotensin-converting enzyme, soluble form (chains A, B) LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAENARRQEEAALL SQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSQMSR IYSTAKVCLPQKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTA LSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDR YINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEF FTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVH HEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTES DINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRN ETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKL RKVLRAGSSRPWQEVLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWH PPLPDNYPEGIDLVTDEAEASKFVEEYD
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
| ZN | Zinc ion | Zn | 2 |
| A1IRR | (2~{S},5~{R})-5-(4-methylphenyl)-1-[2-[[(2~{S})-3-phenyl-2-sulfanyl-propanoyl]a… | C23 H26 N2 O4 S | 2 |
| MG | Magnesium ion | Mg | 3 |
| PE8 | 3,6,9,12,15,18,21-heptaoxatricosane-1,23-diol | C16 H34 O9 | 1 |
Water and common crystallization additives (PG4, ACY, EDO, PGE, CL, PEG) are not listed.
Design of Novel Mercapto-3-phenylpropanoyl Dipeptides as Dual Angiotensin-Converting Enzyme C-Domain-Selective/Neprilysin Inhibitors. Cozier, G.E., Coulson, L.B., Eyermann, C.J. et al. J Med Chem (2025) 68:7720-7736. DOI 10.1021/acs.jmedchem.5c00329 · 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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