7Q26: Angiotensin-1 converting enzyme N-domain

Crystal structure of Angiotensin-1 converting enzyme N-domain in complex with dual ACE/NEP inhibitor AD013. Determined by X-ray diffraction at 1.7 Å resolution. Released 16 Feb 2022.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Homo sapiens
Chains: 2
Atoms: 11,150
Mol. weight: 150.86 kDa
Ligands: ZN, MG, 8JV, PE8
Released: 16 Feb 2022

Explore 7Q26 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7Q26 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.

Chain A: 36 helices, 7 β-strands

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	353-371	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	2
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

Chain B: 36 helices, 7 β-strands

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	126-127	2	4
β-strand	137-138	2	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	280-285	6
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	385-400	16
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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiotensin-converting enzyme	A, B	protein	629	Homo sapiens	P12821 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7Q26_1 Angiotensin-converting enzyme (chains A, B)
LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAENARRQEEAALL
SQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSQMSR
IYSTAKVCLPQKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTA
LSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDR
YINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEF
FTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVH
HEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTES
DINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRN
ETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKL
RKVLRAGSSRPWQEVLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWH
PPLPDNYPEGIDLVTDEAEASKFVEEYDL

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2
MG	Magnesium ion	Mg	2
8JV	(2~{S},5~{R})-5-(4-methylphenyl)-1-[2-[[(2~{S})-1-oxidanyl-1-oxidanylidene-4-ph…	C24 H28 N2 O5	2
PE8	3,6,9,12,15,18,21-heptaoxatricosane-1,23-diol	C16 H34 O9	1
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

Water and common crystallization additives (ACT, CL, PG4, PGE, EDO, PEG, 1PE) are not listed.

Primary citation

Probing the Requirements for Dual Angiotensin-Converting Enzyme C-Domain Selective/Neprilysin Inhibition. Arendse, L.B., Cozier, G.E., Eyermann, C.J. et al. J Med Chem (2022) 65:3371-3387. DOI 10.1021/acs.jmedchem.1c01924 · PubMed

Other PDB entries of the same protein (UniProt P12821 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6H5W 1.37 Å, Crystal structure of human Angiotensin-1 converting enzyme C-domain in complex with…
9H1E 1.45 Å, Crystal structure of Angiotensin-1 converting enzyme C-domain in complex with dual…
7Q27 1.5 Å, Crystal structure of Angiotensin-1 converting enzyme C-domain in complex with dual…
9QAN 1.5 Å, Human angiotensin-1 converting enzyme C-domain in complex with ramiprilat
9QAP 1.5 Å, Human angiotensin-1 converting enzyme C-domain in complex with quinaprilat
5AMB 1.55 Å, Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with…
6F9T 1.6 Å, Crystal structure of human testis Angiotensin-1 converting enzyme in complex with…
7Q25 1.6 Å, Crystal structure of Angiotensin-1 converting enzyme N-domain in complex with dual…
7Q29 1.6 Å, Crystal structure of Angiotensin-1 converting enzyme C-domain in complex with dual…
8QFX 1.6 Å, Human Angiotensin-1 converting enzyme N-domain in complex with the lactotripeptide IPP
5AMC 1.65 Å, Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with…
7Q28 1.65 Å, Crystal structure of Angiotensin-1 converting enzyme C-domain in complex with dual…

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