8I92: ACE2-B0AT1 complex

ACE2-B0AT1 complex bound with glutamine. Determined by electron microscopy at 3.2 Å resolution. Released 27 Sept 2023.

Method

Electron microscopy

Resolution

3.2 Å

Organism

Homo sapiens

Chains

4

Atoms

22,344

Mol. weight

335.36 kDa

Ligands

GLN, ZN, NAG

Released

27 Sept 2023

Explore 8I92 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8I92 contains 170 α-helices and 38 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: 44 helices, 15 β-strands

Molecules and chains

>8I92_1 Angiotensin-converting enzyme 2 (chains A, C)
MRSSSSWLLLSLVAVTAAWSHPQFEKQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYN
TNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSED
KSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSE
VGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFE
EIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNI
DVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDL
GKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLS
AATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKD
QWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQ
AAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPL
FTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAM
RQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRI
NDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKK
NKARSGENPYASIDISKGENNPGFQNTDDVQTSFLEHHHHHHHHHH

>8I92_2 Sodium-dependent neutral amino acid transporter B(0)AT1 (chains B, D)
VLPNPGLDARIPSLAELETIEQEEASSRPKWDNKAQYMLTCLGFCVGLGNVWRFPYLCQS
HGGGAFMIPFLILLVLEGIPLLYLEFAIGQRLRRGSLGVWSSIHPALKGLGLASMLTSFM
VGLYYNTIISWIMWYLFNSFQEPLPWSDCPLNENQTGYVDECARSSPVDYFWYRETLNIS
TSISDSGSIQWWMLLCLACAWSVLYMCTIRGIETTGKAVYITSTLPYVVLTIFLIRGLTL
KGATNGIVFLFTPNVTELAQPDTWLDAGAQVFFSFSLAFGGLISFSSYNSVHNNCEKDSV
IVSIINGFTSVYVAIVVYSVIGFRATQRYDDCFSTNILTLINGFDLPEGNVTQENFVDMQ
QRCNASDPAAYAQLVFQTCDINAFLSEAVEGTGLAFIVFTEAITKMPLSPLWSVLFFIML
FCLGLSSMFGNMEGVVVPLQDLRVIPPKWPKEVLTGLICLGTFLIGFIFTLNSGQYWLSL
LDSYAGSIPLLIIAFCEMFSVVYVYGVDRFNKDIEFMIGHKPNIFWQVTWRVVSPLLMLI
IFLFFFVVEVSQELTYSIWDPGYEEFPKSQKISYPNWVYVVVVIVAGVPSLTIPGYAIYK
LIRNH

Ligands and cofactors

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

Related structures

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

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