8I93: ACE2-B0AT1 complex

ACE2-B0AT1 complex bound with methionine. Determined by electron microscopy at 3.1 Å resolution. Released 27 Sept 2023.

Method: Electron microscopy
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 4
Atoms: 22,342
Mol. weight: 327.93 kDa
Ligands: ZN, MET, NAG
Released: 27 Sept 2023

Explore 8I93 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8I93 contains 148 α-helices and 40 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.

Chains A and C: 38 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	22-51	30
α-helix	56-80	25
α-helix	91-100	10
α-helix	110-129	20
β-strand	131-133	3	1
β-strand	141-143	3	1
β-strand	147	1	1
α-helix	148-154	7
α-helix	158-171	14
α-helix	177-192	16
α-helix	199-203	5
α-helix	204-206	3
β-strand	209	1	2
β-strand	217	1	2
α-helix	221-229	9
α-helix	234-248	15
β-strand	262-263	2	3
α-helix	276-278	3
α-helix	279-282	4
α-helix	294-299	6
α-helix	306-318	13
α-helix	325-330	6
β-strand	332	1	4
β-strand	347-352	6	4
β-strand	355-359	5	4
α-helix	367-382	16
α-helix	390-392	3
α-helix	402-411	10
α-helix	415-421	7
α-helix	434-443	10
α-helix	450-463	14
α-helix	473-480	8
α-helix	481-485	5
β-strand	487-488	2	3
α-helix	500-502	3
α-helix	504-507	4
α-helix	514-530	17
α-helix	539-541	3
α-helix	549-558	10
α-helix	566-571	6
α-helix	582-587	6
α-helix	589-598	10
β-strand	618-622	5	5
α-helix	624-627	4
α-helix	637-657	21
α-helix	667-669	3
β-strand	670-673	4	5
β-strand	680-685	6	5
β-strand	686	1	6
β-strand	694	1	6
α-helix	695-696	2
α-helix	697-715	19
β-strand	722-723	2	5
α-helix	742-766	25

Chains B and D: 36 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	21-24	4
α-helix	25-29	5
α-helix	38-48	11
α-helix	58-63	6
α-helix	72-77	6
α-helix	78-82	5
α-helix	83-95	13
α-helix	109-111	3
α-helix	114-128	15
α-helix	131-141	11
α-helix	149-151	3
α-helix	153-154	2
β-strand	155	1	7
β-strand	162	1	7
α-helix	164-167	4
α-helix	173-175	3
α-helix	176-180	5
α-helix	195-211	17
α-helix	219-226	8
α-helix	230-242	13
α-helix	265-278	14
α-helix	286-289	4
α-helix	299-313	15
α-helix	315-348	34
α-helix	352-354	3
α-helix	360-368	9
α-helix	372-375	4
α-helix	413-444	32
α-helix	455-469	15
α-helix	479-507	29
α-helix	511-522	12
α-helix	525-527	3
α-helix	528-532	5
α-helix	533-537	5
α-helix	538-550	13
β-strand	559-562	4	8
α-helix	573	1
β-strand	574-577	4	8
α-helix	582-590	9
α-helix	592-607	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiotensin-converting enzyme 2	A, C	protein	749	Homo sapiens	Q9BYF1 (AlphaFold model)
Sodium-dependent neutral amino acid transporter B(0)AT1	B, D	protein	653	Homo sapiens	Q695T7 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>8I93_1 Angiotensin-converting enzyme 2 (chains A, C)
TIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTL
AQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQ
ECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDY
GDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPI
GCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVG
LPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHI
QYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFL
LKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCD
PASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLR
LGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIK
VRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRI
SFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPV
SIWLIVFGVVMGVIVVGIVILIFTGIRDR

Sequence of entity 2 (B, D), FASTA

>8I93_2 Sodium-dependent neutral amino acid transporter B(0)AT1 (chains B, D)
MADYKDDDDKSGPDEVDASGRVRLVLPNPGLDARIPSLAELETIEQEEASSRPKWDNKAQ
YMLTCLGFCVGLGNVWRFPYLCQSHGGGAFMIPFLILLVLEGIPLLYLEFAIGQRLRRGS
LGVWSSIHPALKGLGLASMLTSFMVGLYYNTIISWIMWYLFNSFQEPLPWSDCPLNENQT
GYVDECARSSPVDYFWYRETLNISTSISDSGSIQWWMLLCLACAWSVLYMCTIRGIETTG
KAVYITSTLPYVVLTIFLIRGLTLKGATNGIVFLFTPNVTELAQPDTWLDAGAQVFFSFS
LAFGGLISFSSYNSVHNNCEKDSVIVSIINGFTSVYVAIVVYSVIGFRATQRYDDCFSTN
ILTLINGFDLPEGNVTQENFVDMQQRCNASDPAAYAQLVFQTCDINAFLSEAVEGTGLAF
IVFTEAITKMPLSPLWSVLFFIMLFCLGLSSMFGNMEGVVVPLQDLRVIPPKWPKEVLTG
LICLGTFLIGFIFTLNSGQYWLSLLDSYAGSIPLLIIAFCEMFSVVYVYGVDRFNKDIEF
MIGHKPNIFWQVTWRVVSPLLMLIIFLFFFVVEVSQELTYSIWDPGYEEFPKSQKISYPN
WVYVVVVIVAGVPSLTIPGYAIYKLIRNHCQKPGDHQGLVSTLSTASMNGDLK

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2
MET	Methionine	C5 H11 N O2 S	2
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	10

Primary citation

Structural insight into the substrate recognition and transport mechanism of amino acid transporter complex ACE2-B 0 AT1 and ACE2-SIT1. Li, Y., Chen, Y., Zhang, Y. et al. Cell Discov (2023) 9:93-93. DOI 10.1038/s41421-023-00596-2 · 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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