9VA2: ACE2-B0AT1

Structure of the ACE2-B0AT1 bound with Phenylalanine. Determined by electron microscopy at 2.87 Å resolution. Released 13 May 2026.

Method: Electron microscopy
Resolution: 2.87 Å
Organism: Homo sapiens
Chains: 4
Atoms: 22,094
Mol. weight: 337.87 kDa
Ligands: NAG, PHE
Released: 13 May 2026

Explore 9VA2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9VA2 contains 157 α-helices and 44 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: 43 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	21-52	32
α-helix	56-80	25
α-helix	95-98	4
α-helix	110-129	20
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	174-192	19
α-helix	199-204	6
α-helix	205-207	3
β-strand	209	1	2
β-strand	217	1	2
α-helix	221-230	10
α-helix	234-248	15
β-strand	260	1	3
β-strand	262-263	2	4
α-helix	264-266	3
α-helix	276-278	3
α-helix	279-282	4
α-helix	289-291	3
α-helix	294-299	6
α-helix	306-317	12
α-helix	325-329	5
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	401-410	10
α-helix	415-420	6
α-helix	432-446	15
α-helix	450-463	14
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	514-530	17
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
β-strand	607	1	3
β-strand	618-620	3	6
β-strand	621-622	2	7
α-helix	624-627	4
α-helix	632-634	3
α-helix	637-657	21
α-helix	667-669	3
β-strand	670-673	4	6
β-strand	681-685	5	6
β-strand	686	1	8
β-strand	694	1	8
α-helix	695-696	2
α-helix	697-713	17
β-strand	722-723	2	7
α-helix	741-766	26

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

Element	Residues	Length	Sheet
α-helix	21-24	4
α-helix	38-47	10
α-helix	57-64	8
α-helix	71-96	26
α-helix	102-105	4
α-helix	109-111	3
α-helix	112-141	30
β-strand	155	1	9
β-strand	162	1	9
α-helix	164-168	5
α-helix	171-174	4
α-helix	175-181	7
α-helix	195-211	17
α-helix	219-226	8
α-helix	229-243	15
α-helix	251-254	4
α-helix	265-278	14
α-helix	284-289	6
α-helix	299-348	50
α-helix	360-370	11
α-helix	372-377	6
α-helix	398-402	5
α-helix	403-407	5
α-helix	413-435	23
α-helix	441-444	4
α-helix	455-469	15
α-helix	472-474	3
α-helix	478-489	12
α-helix	493-507	15
α-helix	511-522	12
α-helix	525-527	3
α-helix	528-532	5
α-helix	533-537	5
α-helix	538-551	14
β-strand	559-562	4	10
β-strand	574-577	4	10
α-helix	581-584	4
α-helix	585-586	2
α-helix	587-591	5
α-helix	592-607	16

Chain C: 42 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	21-52	32
α-helix	56-80	25
α-helix	95-98	4
α-helix	110-129	20
β-strand	131-133	3	11
β-strand	141-143	3	11
α-helix	144-148	5
α-helix	149-154	6
α-helix	158-168	11
α-helix	169-173	5
α-helix	174-192	19
α-helix	199-204	6
α-helix	205-207	3
β-strand	209	1	12
β-strand	217	1	12
α-helix	221-230	10
α-helix	234-248	15
β-strand	260	1	13
β-strand	262-263	2	14
α-helix	264-266	3
α-helix	276-278	3
α-helix	279-282	4
α-helix	289-291	3
α-helix	294-299	6
α-helix	306-317	12
α-helix	325-329	5
β-strand	332	1	15
β-strand	347-352	6	15
β-strand	355-359	5	15
α-helix	366-384	19
α-helix	390-392	3
α-helix	401-410	10
α-helix	415-420	6
α-helix	432-446	15
α-helix	450-463	14
α-helix	473-480	8
α-helix	481-485	5
β-strand	487-488	2	14
α-helix	500-502	3
α-helix	514-530	17
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
β-strand	607	1	13
β-strand	618-620	3	16
β-strand	621-622	2	17
α-helix	624-627	4
α-helix	632-634	3
α-helix	637-657	21
α-helix	667-669	3
β-strand	670-673	4	16
β-strand	681-685	5	16
β-strand	686	1	18
β-strand	694	1	18
α-helix	695-696	2
α-helix	697-713	17
β-strand	722-723	2	17
α-helix	742-766	25

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiotensin-converting enzyme 2	A, C	protein	808	Homo sapiens	Q9BYF1 (AlphaFold model)
Sodium-dependent neutral amino acid transporter B(0)AT1	B, D	protein	652	Homo sapiens	Q695T7 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>9VA2_1 Angiotensin-converting enzyme 2 (chains A, C)
WSHPQFEKQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKW
SAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYST
GKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNE
MARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLM
NAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFK
EAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDF
LTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQ
EDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVE
PVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTE
AGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTD
WSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEED
VRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQP
TLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENPYASIDISKG
ENNPGFQNTDDVQTSFLEHHHHHHHHHH

Sequence of entity 2 (B, D), FASTA

>9VA2_2 Sodium-dependent neutral amino acid transporter B(0)AT1 (chains B, D)
DYKDDDDKSGPDEVDASGRVRLVLPNPGLDARIPSLAELETIEQEEASSRPKWDNKAQYM
LTCLGFCVGLGNVWRFPYLCQSHGGGAFMIPFLILLVLEGIPLLYLEFAIGQRLRRGSLG
VWSSIHPALKGLGLASMLTSFMVGLYYNTIISWIMWYLFNSFQEPLPWSDCPLNENQTGY
VDECARSSPVDYFWYRETLNISTSISDSGSIQWWMLLCLACAWSVLYMCTIRGIETTGKA
VYITSTLPYVVLTIFLIRGLTLKGATNGIVFLFTPNVTELAQPDTWLDAGAQVFFSFSLA
FGGLISFSSYNSVHNNCEKDSVIVSIINGFTSVYVAIVVYSVIGFRATQRYDDCFSTNIL
TLINGFDLPEGNVTQENFVDMQQRCNASDPAAYAQLVFQTCDINAFLSEAVEGTGLAFIV
FTEAITKMPLSPLWSVLFFIMLFCLGLSSMFGNMEGVVVPLQDLRVIPPKWPKEVLTGLI
CLGTFLIGFIFTLNSGQYWLSLLDSYAGSIPLLIIAFCEMFSVVYVYGVDRFNKDIEFMI
GHKPNIFWQVTWRVVSPLLMLIIFLFFFVVEVSQELTYSIWDPGYEEFPKSQKISYPNWV
YVVVVIVAGVPSLTIPGYAIYKLIRNHCQKPGDHQGLVSTLSTASMNGDLKY

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	12
PHE	Phenylalanine	C9 H11 N O2	2

Primary citation

Structural basis of aromatic amino acid recognition by the human ACE2-B0AT1 transporter complex. Zhang, T., Zeng, Q., Xu, C. et al. Oral Science And Homeostatic Medicine (2025) 1:9610033. DOI 10.26599/OSHM.2025.9610033

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

Browse structure collections

About this viewer

MolViewer shows 9VA2 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.