1R42: Angiotensin I converting enzyme 2

Native Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2). Determined by X-ray diffraction at 2.2 Å resolution. Released 3 Feb 2004.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 5
Atoms: 5,511
Mol. weight: 76.77 kDa
Ligands: NAG, ZN
Released: 3 Feb 2004

Explore 1R42 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1R42 contains 39 α-helices and 15 β-strands across 5 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: 37 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	23-52	30
α-helix	56-77	22
α-helix	91-100	10
α-helix	104-107	4
α-helix	110-129	20
β-strand	131-134	4	1
β-strand	137-143	7	1
β-strand	147	1	1
α-helix	148-154	7
α-helix	158-167	10
α-helix	168-173	6
α-helix	174-193	20
α-helix	199-204	6
β-strand	209	1	2
β-strand	217	1	2
α-helix	220-251	32
β-strand	260	1	3
α-helix	261	1
β-strand	262-263	2	4
α-helix	264-266	3
α-helix	276-278	3
α-helix	279-282	4
α-helix	298-300	3
α-helix	304-316	13
α-helix	320-324	5
α-helix	327-330	4
β-strand	332	1	5
β-strand	347-352	6	5
β-strand	355-359	5	5
α-helix	366-384	19
α-helix	390-392	3
α-helix	400-413	14
α-helix	415-420	6
α-helix	429-431	3
α-helix	432-446	15
α-helix	449-465	17
α-helix	470-472	3
α-helix	473-480	8
α-helix	481-485	5
β-strand	487-488	2	4
α-helix	499-502	4
α-helix	504-507	4
α-helix	514-531	18
α-helix	539-541	3
α-helix	548-558	11
α-helix	566-574	9
α-helix	582-598	17
α-helix	603-604	2
β-strand	607	1	3

Chain B: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	902	1	6

Chain C: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	909-912	4	6

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	928-942	15

Chain E: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	950-952	3
β-strand	953-956	4	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
angiotensin I converting enzyme 2	A	protein	615	Homo sapiens	Q9BYF1 (AlphaFold model)
disordered segment of collectrin homology domain	B	protein	6	Homo sapiens
disordered segment of collectrin homology domain	C	protein	20	Homo sapiens
disordered segment of collectrin homology domain	D	protein	18	Homo sapiens
disordered segment of collectrin homology domain	E	protein	14	Homo sapiens

Sequence of entity 1 (A), FASTA

>1R42_1 angiotensin I converting enzyme 2 (chains A)
MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQ
NMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTIL
NTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLY
EEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHL
HAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQ
AWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILM
CTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKS
IGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEM
KREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLH
KCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNK
NSFVGWSTDWSPYAD

Sequence of entity 2 (B), FASTA

>1R42_2 disordered segment of collectrin homology domain (chains B)
XXXXXX

Sequence of entity 3 (C), FASTA

>1R42_3 disordered segment of collectrin homology domain (chains C)
XXXXXXXXXXXXXXXXXXXX

Sequence of entity 4 (D), FASTA

>1R42_4 disordered segment of collectrin homology domain (chains D)
XXXXXXXXXXXXXXXXXX

Sequence of entity 5 (E), FASTA

>1R42_5 disordered segment of collectrin homology domain (chains E)
XXXXXXXXXXXXXX

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	3
ZN	Zinc ion	Zn	1

Water and common crystallization additives (CL) are not listed.

Primary citation

ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis. Towler, P., Staker, B., Prasad, S.G. et al. J Biol Chem (2004) 279:17996-18007. DOI 10.1074/jbc.M311191200 · PubMed

Other PDB entries of the same protein (UniProt Q9BYF1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9SPA 1.79 Å, Apo ACE2 extracellular domain
28KD 2.02 Å, ACE2 extracellular domain in complex with the macrocyclic peptide GR3.1.2
8BYJ 2.07 Å, The structures of Ace2 in complex with bicyclic peptide inhibitor
8B9P 2.11 Å, ACE2 in complex with bicyclic peptide inhibitor
8XSF 2.16 Å, SARS-CoV-2 rbd + imcas-364 + hACE2
7JVO 2.2 Å, Importin alpha bound to the C-terminus of ACE2
8TOR 2.2 Å, ACE2-peptide 2 complex
9RVA 2.2 Å, Crystal structure of the extracellular part of human ACE2 in complex with the…
9UE7 2.27 Å, Cryo-EM structure of SARS-CoV-2 KP.2 spike in complex with ACE2
8TOQ 2.3 Å, ACE2-peptide 1 complex
8BFW 2.33 Å, The structures of Ace2 in complex with bicyclic peptide inhibitor
8TOS 2.35 Å, ACE2-peptide 6 complex

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