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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Cryo-EM structure of Rc-o319 RBD/R. cornutus ACE2 complex | |||||||||
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![]() | Rhinolophus cornutus / Coronavirinae / VIRAL PROTEIN | |||||||||
Function / homology | ![]() Hydrolases; Acting on peptide bonds (peptidases) / peptidyl-dipeptidase activity / carboxypeptidase activity / metallopeptidase activity / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated virion attachment to host cell / cilium / apical plasma membrane / endocytosis involved in viral entry into host cell / fusion of virus membrane with host plasma membrane ...Hydrolases; Acting on peptide bonds (peptidases) / peptidyl-dipeptidase activity / carboxypeptidase activity / metallopeptidase activity / host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated virion attachment to host cell / cilium / apical plasma membrane / endocytosis involved in viral entry into host cell / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / host cell plasma membrane / virion membrane / proteolysis / extracellular space / metal ion binding / membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.79 Å | |||||||||
![]() | Matsumoto K / Shihoya W / Nureki O | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular basis of sarbecovirus evolution and receptor tropism in natural hosts, potential intermediate hosts, and humans. Authors: Kosugi Y / Matsumoto K / Lytras S / Plianchaisuk A / Tolentino EJ / Fujita S / Yo SM / Luo C / Kim Y / Shihoya W / Ito J / Nureki O / Sato K | |||||||||
History |
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 17.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.9 KB 16.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 6.9 KB | Display | ![]() |
Images | ![]() | 44.8 KB | ||
Masks | ![]() | 35.3 MB | ![]() | |
Filedesc metadata | ![]() | 6.8 KB | ||
Others | ![]() ![]() | 32.8 MB 32.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 703.8 KB | Display | ![]() |
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Full document | ![]() | 703.4 KB | Display | |
Data in XML | ![]() | 14.5 KB | Display | |
Data in CIF | ![]() | 18.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9m3fMC ![]() 9vg7C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 1.1067 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Rc-o319 RBD and R. cornutus ACE2 complex
Entire | Name: Rc-o319 RBD and R. cornutus ACE2 complex |
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Components |
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-Supramolecule #1: Rc-o319 RBD and R. cornutus ACE2 complex
Supramolecule | Name: Rc-o319 RBD and R. cornutus ACE2 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 99.73 kDa/nm |
-Macromolecule #1: Angiotensin-converting enzyme
Macromolecule | Name: Angiotensin-converting enzyme / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: Hydrolases; Acting on peptide bonds (peptidases) |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 69.564234 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: STTEDEAKKF LNDFNSEAEN LTYQSSLASW DYNTNISDEN VQKMDEAGAK WSAFYEEQSK IAKNYPLEEI QTDIVKRQLQ ILQQSGSPV LSEDKSKRLN SILNAMSTIY STGKVCKPNN PQECLLLEPG LDNIMGTSKD YHERLWAWEG WRAEVGKQLR P LYEEYVVL ...String: STTEDEAKKF LNDFNSEAEN LTYQSSLASW DYNTNISDEN VQKMDEAGAK WSAFYEEQSK IAKNYPLEEI QTDIVKRQLQ ILQQSGSPV LSEDKSKRLN SILNAMSTIY STGKVCKPNN PQECLLLEPG LDNIMGTSKD YHERLWAWEG WRAEVGKQLR P LYEEYVVL KNEMARGYHY EDYGDYWRRD YETEESSGPG YSRDQLMKDV DRIFTEIKPL YEHLHAYVRA KLMDTYPLHI SP TGCLPAH LLGDMWGRFW TNLYPLTVPF GQKPNIDVTD EMVKQGWDAN RIFKEAEKFF VSVGLPNMTE GFWNNSMLTE PGD GRKVVC HPTAWDLGKG DFRIKMCTKV TMEDFLTAHH EMGHIQYDMA YASQPYLLRN GANEGFHEAV GEVMSLSVAT PKHL KTMGL LSPDFREDDE TEINFLLKQA LNIVGTLPFT YMLEKWRWMV FKGEIPKEEW MKKWWEMRRE IVGVVEPVPH DETYC DPAS LFHVANDYSF IRYYTRTIFE FQFHEALCRI AQHNGPLHKC DISNSTDAGK KLHQMLSVGK SQAWTKTLED IVGSRN MDV GPLLRYFEPL YTWLQEQNRK SYVGWNTDWS PYSD UniProtKB: Angiotensin-converting enzyme |
-Macromolecule #2: Spike glycoprotein
Macromolecule | Name: Spike glycoprotein / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 133.626016 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: EFKLATMGIL PSPGMPALLS LVSLLSVLLM GCVAETGVYG CVNITYGSHH LYVSSRTRGV YYPDDAFRSS TNVLHEGFFL PFDSNVTWY SFWNQKYSVA TSPFGDGVYF STIDKSNVVR GWVFGTTLDN DTQSVLLYND GTHVRVEVCT FHFCPTPVFS A SSPHLYSS ...String: EFKLATMGIL PSPGMPALLS LVSLLSVLLM GCVAETGVYG CVNITYGSHH LYVSSRTRGV YYPDDAFRSS TNVLHEGFFL PFDSNVTWY SFWNQKYSVA TSPFGDGVYF STIDKSNVVR GWVFGTTLDN DTQSVLLYND GTHVRVEVCT FHFCPTPVFS A SSPHLYSS AFNCTLNYTL ASVRADFTEV DGSFKTIREF VFKLQDGSLN VYYASTSYVL AIGATSQLPS GVTPLVPLWK IP IGLNITN FKTLVYLRSD NTPLQAAYVV GHLKRRTMMF KYDENGTIVD AIDCALDPLS ETKCTLRSFI VEKGIYQTSN FRV QPQDTV VRFPNITNLC PFSEVFNATT FASVYAWNRK RISNCVADYS VLYNSTSFST FQCYGVSSTK LNDLCFTNVY ADSF VVRGD EVRQIAPGQT GVIADYNYKL PDDFTGCVLA WNSRNQDAST SGNFNYYYRI WRSEKLRPFE RDIAHYDYQV GTQFK SSLK NYGFYSSAGD SHQPYRVVVL SFELLNAPAT VCGPKQSTEL IKNKCVNFNF NGLTGTGVLT DSNKKFQSFQ QFGRDV SDF TDSVKDPKTL EVLDITPCSY GGVSVITPGT NASTQVAVLY QDVNCTDVPT AIHAEQLTPS WRVYSTGTNM FQTQAGC LI GAEHVNNSYD CDIPIGAGIC ATYHTPSMLR SANNNKRIVA YVMSLGAENS VAYSNNTIAI PTNFTISVTT EVMPVSMT K TSVDCTMYIC GDSVECSTLL LQYGSFCTQL NRALTGIAVE QDKNTQEVFA QVKQIYKTPD IKDFGGFNFS QILPDPSKP SKRSPIEDLL FNKVTLADAG FVKQYGDCLG DIQARDLICA QKFNGLTVLP PLLTDEMIAA YTAALISGTA TAGWTFGAGP ALQIPFPMQ MAYRFNGIGV TQNVLYENQK LIANQFNSAI GKIQESLTST PSALGKLQDV VNQNAQALNT LVKQLSSNFG A ISSVLNDI ISRLDPPEAE VQIDRLITGR LQSLQTYVTQ QLIRAAEIRA SANLAATKMS ECVLGQSKRV DFCGKGYHLM SF PQAAPHG VVFLHVTYIP SQERNFTTAP AICHEGKAHF PREGVFVSNG THWFITQRNF YEPQIITTDN TFVSGTCDVV IGI VNNTVY DPLQPELESF KDELDKYFKN HTSPDIDLGD ISGINASVVD IQKEIDILKD VAKNLNESLI NLQELGKYEQ YIGT KHHHH HH UniProtKB: Spike glycoprotein |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 49.9 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |