6M18: ACE2-B0AT1 complex

ACE2-B0AT1 complex. Determined by electron microscopy at 2.9 Å resolution. Released 11 Mar 2020.

Method: Electron microscopy
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 4
Atoms: 22,534
Mol. weight: 345.2 kDa
Ligands: NAG, 3PH, ZN
Released: 11 Mar 2020

Explore 6M18 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6M18 contains 154 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: 32 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	21-24	4
α-helix	39-49	11
α-helix	58-64	7
α-helix	71-77	7
α-helix	78-82	5
α-helix	83-96	14
α-helix	101-104	4
α-helix	113-141	29
α-helix	153-154	2
β-strand	155	1	1
β-strand	162	1	1
α-helix	164-168	5
α-helix	171-177	7
α-helix	195-211	17
α-helix	219-241	23
α-helix	251-254	4
α-helix	259-262	4
α-helix	267-278	12
α-helix	286-290	5
α-helix	300-348	49
α-helix	361-370	10
α-helix	397-400	4
α-helix	403-408	6
α-helix	413-440	28
α-helix	442-445	4
α-helix	455-469	15
α-helix	472-474	3
α-helix	478-503	26
α-helix	504-510	7
α-helix	511-522	12
α-helix	528-532	5
α-helix	533-537	5
α-helix	538-552	15
α-helix	582-607	26

Chains B and D: 45 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	22-52	31
α-helix	59-79	21
α-helix	80-82	3
α-helix	91-101	11
α-helix	104-107	4
α-helix	112-129	18
β-strand	131-133	3	2
β-strand	141-143	3	2
α-helix	144-148	5
α-helix	149-154	6
α-helix	158-192	35
α-helix	199-203	5
α-helix	204-207	4
β-strand	209	1	3
β-strand	217	1	3
α-helix	221-248	28
β-strand	260	1	4
α-helix	261	1
β-strand	262-263	2	5
α-helix	264-266	3
α-helix	276-278	3
α-helix	279-282	4
α-helix	289-291	3
α-helix	296-299	4
α-helix	306-317	12
α-helix	325-329	5
β-strand	332	1	6
β-strand	347-350	4	6
β-strand	356-359	4	6
α-helix	366-382	17
α-helix	390-392	3
α-helix	401-411	11
α-helix	415-421	7
α-helix	429-431	3
α-helix	434-445	12
α-helix	450-465	16
α-helix	470-472	3
α-helix	473-480	8
α-helix	481-485	5
β-strand	487-488	2	5
α-helix	499-502	4
α-helix	504-507	4
α-helix	514-532	19
α-helix	539-541	3
α-helix	550-558	9
α-helix	566-571	6
α-helix	582-587	6
α-helix	589-598	10
β-strand	607	1	4
β-strand	618-622	5	7
α-helix	624-627	4
α-helix	637-657	21
α-helix	667-669	3
β-strand	670-673	4	7
β-strand	680-685	6	7
β-strand	686-687	2	8
β-strand	690-694	5	8
α-helix	695-696	2
α-helix	697-706	10
α-helix	708-715	8
β-strand	722-723	2	7
α-helix	742-761	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Sodium-dependent neutral amino acid transporter B(0)AT1	A, C	protein	654	Homo sapiens	Q695T7 (AlphaFold model)
Angiotensin-converting enzyme 2	B, D	protein	814	Homo sapiens	Q9BYF1 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6M18_1 Sodium-dependent neutral amino acid transporter B(0)AT1 (chains A, C)
MADYKDDDDKSGPDEVDASGRVRLVLPNPGLDARIPSLAELETIEQEEASSRPKWDNKAQ
YMLTCLGFCVGLGNVWRFPYLCQSHGGGAFMIPFLILLVLEGIPLLYLEFAIGQRLRRGS
LGVWSSIHPALKGLGLASMLTSFMVGLYYNTIISWIMWYLFNSFQEPLPWSDCPLNENQT
GYVDECARSSPVDYFWYRETLNISTSISDSGSIQWWMLLCLACAWSVLYMCTIRGIETTG
KAVYITSTLPYVVLTIFLIRGLTLKGATNGIVFLFTPNVTELAQPDTWLDAGAQVFFSFS
LAFGGLISFSSYNSVHNNCEKDSVIVSIINGFTSVYVAIVVYSVIGFRATQRYDDCFSTN
ILTLINGFDLPEGNVTQENFVDMQQRCNASDPAAYAQLVFQTCDINAFLSEAVEGTGLAF
IVFTEAITKMPLSPLWSVLFFIMLFCLGLSSMFGNMEGVVVPLQDLRVIPPKWPKEVLTG
LICLGTFLIGFIFTLNSGQYWLSLLDSYAGSIPLLIIAFCEMFSVVYVYGVDRFNKDIEF
MIGHKPNIFWQVTWRVVSPLLMLIIFLFFFVVEVSQELTYSIWDPGYEEFPKSQKISYPN
WVYVVVVIVAGVPSLTIPGYAIYKLIRNHCQKPGDHQGLVSTLSTASMNGDLKY

Sequence of entity 2 (B, D), FASTA

>6M18_2 Angiotensin-converting enzyme 2 (chains B, D)
MRSSSSWLLLSLVAVTAAWSHPQFEKQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYN
TNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSED
KSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSE
VGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFE
EIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNI
DVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDL
GKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLS
AATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKD
QWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQ
AAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPL
FTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAM
RQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRI
NDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKK
NKARSGENPYASIDISKGENNPGFQNTDDVQTSF

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	10
3PH	1,2-diacyl-glycerol-3-sn-phosphate	C39 H77 O8 P	4
ZN	Zinc ion	Zn	2

Primary citation

Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Yan, R., Zhang, Y., Li, Y. et al. Science (2020) 367:1444-1448. DOI 10.1126/science.abb2762 · PubMed

Other PDB entries of the same protein (UniProt Q695T7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9KXW 2.66 Å, Structure of human B0AT1-ACE2
9KY0 2.68 Å, Structure of human B0AT1-ACE2 complex with compound3
9KXT 2.7 Å, Structure of human B0AT1-ACE2 complex with compound1
9KXV 2.71 Å, Structure of human B0AT1-ACE2 complex with compound3
9KXX 2.77 Å, Inward-open Structure of human B0AT1
9KXZ 2.8 Å, Structure of human B0AT1-ACE2 complex with compound1
9KY1 2.8 Å, Structure of human B0AT1-ACE2 complex with compound1
9KXY 2.82 Å, Structure of human B0AT1-ACE2 complex with compound1
9KXU 2.87 Å, Structure of human B0AT1-ACE2 complex with compound 2
9VA2 2.87 Å, Structure of the ACE2-B0AT1 bound with Phenylalanine
6M17 2.9 Å, The 2019-nCoV RBD/ACE2-B0AT1 complex
8I93 3.1 Å, ACE2-B0AT1 complex bound with methionine

Browse structure collections

About this viewer

MolViewer shows 6M18 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.