7DRV: Angiotensin-converting enzyme 2

Structural basis of SARS-CoV-2-closely-related bat coronavirus RaTG13 to hACE2. Determined by X-ray diffraction at 3.09 Å resolution. Released 25 Aug 2021.

Method: X-ray diffraction
Resolution: 3.09 Å
Organisms: Homo sapiens, Bat coronavirus RaTG13
Chains: 4
Atoms: 12,916
Mol. weight: 190.89 kDa
Ligands: ZN, NAG
Released: 25 Aug 2021

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

Secondary structure: helices and β-sheets

7DRV contains 101 α-helices and 52 β-strands across 4 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: 42 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	21-52	32
α-helix	56-80	25
α-helix	85-87	3
α-helix	91-101	11
α-helix	104-106	3
α-helix	112-129	18
β-strand	131-133	3	1
β-strand	141-143	3	1
α-helix	144-148	5
α-helix	149-154	6
α-helix	158-168	11
α-helix	169-173	5
α-helix	174-193	20
α-helix	199-203	5
α-helix	204-207	4
β-strand	209	1	2
β-strand	217	1	2
α-helix	220-231	12
α-helix	234-251	18
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	289-290	2
α-helix	294-299	6
α-helix	304-316	13
α-helix	320-324	5
α-helix	325-330	6
β-strand	347-352	6	5
β-strand	355-359	5	5
α-helix	366-384	19
α-helix	385-387	3
α-helix	390-392	3
α-helix	400-413	14
α-helix	415-418	4
α-helix	432-445	14
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	500-502	3
α-helix	504-507	4
α-helix	514-531	18
α-helix	539-541	3
α-helix	548-558	11
α-helix	566-571	6
α-helix	582-587	6
α-helix	589-598	10
β-strand	607	1	3

Chain B: 41 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	21-52	32
α-helix	60-80	21
α-helix	91-101	11
α-helix	104-106	3
α-helix	110-129	20
β-strand	132-133	2	12
β-strand	141-142	2	12
α-helix	144-148	5
α-helix	149-154	6
α-helix	158-171	14
α-helix	177-192	16
α-helix	199-203	5
α-helix	204-207	4
β-strand	209	1	13
β-strand	217	1	13
α-helix	221-230	10
α-helix	234-251	18
β-strand	260	1	14
α-helix	261	1
β-strand	262-263	2	15
α-helix	264-266	3
α-helix	276-278	3
α-helix	279-282	4
α-helix	294-299	6
α-helix	304-317	14
α-helix	320-324	5
α-helix	325-330	6
β-strand	347-352	6	16
β-strand	355-359	5	16
α-helix	366-384	19
α-helix	385-387	3
α-helix	390-392	3
α-helix	398-404	7
α-helix	406-412	7
α-helix	415-421	7
α-helix	432-445	14
α-helix	450-464	15
α-helix	470-472	3
α-helix	473-480	8
α-helix	481-485	5
β-strand	487-488	2	15
α-helix	500-502	3
α-helix	504-507	4
α-helix	514-532	19
α-helix	539-541	3
α-helix	548-558	11
α-helix	566-574	9
α-helix	582-587	6
α-helix	589-598	10
α-helix	599-601	3
β-strand	607	1	14

Chain C: 8 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	6
α-helix	21-24	4
β-strand	31	1	7
α-helix	32-34	3
β-strand	36-40	5	7
β-strand	44	1	6
α-helix	48-51	4
β-strand	58-61	4	7
β-strand	74	1	8
β-strand	76-84	9	7
α-helix	89-91	3
α-helix	99-104	6
β-strand	113-119	7	7
β-strand	130	1	9
β-strand	134-136	3	10
α-helix	142-144	3
α-helix	153-154	2
β-strand	155-156	2	11
β-strand	167	1	11
β-strand	170-171	2	11
β-strand	174-176	3	10
β-strand	179	1	9
α-helix	185-187	3
β-strand	190-198	9	7
β-strand	206	1	8

Chain D: 10 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	16-18	3
α-helix	29-31	3
α-helix	32-34	3
β-strand	36	1	17
β-strand	39-40	2	18
α-helix	47-49	3
β-strand	58-61	4	17
β-strand	74	1	19
β-strand	77-78	2	18
β-strand	79-85	7	17
α-helix	86-91	6
α-helix	100-104	5
β-strand	113-119	7	17
β-strand	130	1	20
β-strand	134-136	3	21
α-helix	142-144	3
α-helix	154	1
β-strand	155-156	2	22
β-strand	170-171	2	22
β-strand	174-176	3	21
β-strand	179	1	20
α-helix	185-187	3
β-strand	189-196	8	17
α-helix	197	1
β-strand	206	1	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiotensin-converting enzyme 2	A, B	protein	596	Homo sapiens	Q9BYF1 (AlphaFold model)
Spike glycoprotein	C, D	protein	223	Bat coronavirus RaTG13	A0ABF7PLN6

Sequence of entity 1 (A, B), FASTA

>7DRV_1 Angiotensin-converting enzyme 2 (chains A, B)
STIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQST
LAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNP
QECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYED
YGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISP
IGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSV
GLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGH
IQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINF
LLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYC
DPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNML
RLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYA

Sequence of entity 2 (C, D), FASTA

>7DRV_2 Spike glycoprotein (chains C, D)
RVQPTDSIVRFPNITNLCPFGEVFNATTFASVYAWNRKRISNCVADYSVLYNSTSFSTFK
CYGVSPTKLNDLCFTNVYADSFVITGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNS
KHIDAKEGGNFNYLYRLFRKANLKPFERDISTEIYQAGSKPCNGQTGLNCYYPLYRYGFY
PTDGVGHQPYRVVVLSFELLNAPATVCGPKKSTNLVKNKCVNF

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	5

Primary citation

Binding and molecular basis of the bat coronavirus RaTG13 virus to ACE2 in humans and other species. Liu, K., Pan, X., Li, L. et al. Cell (2021) 184:3438-3451.e10. DOI 10.1016/j.cell.2021.05.031 · 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
1R42 2.2 Å, Native Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2)
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

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