7Z6Z: Angiotensin-1 converting enzyme N-domain

Crystal structure of Angiotensin-1 converting enzyme N-domain in complex with fosinoprilat. Determined by X-ray diffraction at 1.75 Å resolution. Released 22 Jun 2022.

Method: X-ray diffraction
Resolution: 1.75 Å
Organism: Homo sapiens
Chains: 2
Atoms: 11,194
Mol. weight: 151.91 kDa
Ligands: KS8, ZN, NAG, CA
Released: 22 Jun 2022

Explore 7Z6Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7Z6Z contains 73 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	353-372	20
α-helix	377-379	3
α-helix	385-399	15
α-helix	402-407	6
α-helix	418-432	15
α-helix	436-451	16
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: 37 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	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	385-400	16
α-helix	402-407	6
α-helix	412-415	4
α-helix	418-432	15
α-helix	436-451	16
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, soluble form	A, B	protein	628	Homo sapiens	P12821 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7Z6Z_1 Angiotensin-converting enzyme, soluble form (chains A, B)
LDPGLQPGQFSADEAGAQLFAQSYQSSAEQVLFQSVAASWAHDTNITAENARRQEEAALL
SQEFAEAWGQKAKELYEPIWQQFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSQMSR
IYSTAKVCLPQKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTA
LSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDR
YINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWQATHMFRVAEEF
FTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVH
HEMGHIQYYLQYKDLPVSLRRGANPGFHEAIGDVLALSVSTPEHLHKIGLLDRVTNDTES
DINYLLKMALEKIAFLPFGYLVDQWRWGVFSGRTPPSRYNFDWWYLRTKYQGICPPVTRN
ETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYRSTKAGAKL
RKVLRAGSSRPWQEVLKDMVGLDALDAQPLLKYFQLVTQWLQEQNQQNGEVLGWPEYQWH
PPLPDNYPEGIDLVTDEAEASKFVEEYD

Ligands and cofactors

ID	Name	Formula	Copies
KS8	fosinoprilat	C23 H34 N O5 P	2
ZN	Zinc ion	Zn	2
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1
CA	Calcium ion	Ca	3

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

Primary citation

Structural basis for the inhibition of human angiotensin-1 converting enzyme by fosinoprilat. Cozier, G.E., Newby, E.C., Schwager, S.L.U. et al. FEBS J (2022) 289:6659-6671. DOI 10.1111/febs.16543 · 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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