› › Structure analysis

Cryo-EM structure of SARS-CoV-2 D614G S with two ACE2 receptors binding (RB2) in prefusion conformation

Electron Microscopy
3.4Å resolution
PDB entry 8z4x coloured by chain, front view.
PDB entry 8z4x coloured by chain, side view.
PDB entry 8z4x coloured by chain, top view.
Source organisms:
Assembly composition:
hetero pentamer (preferred)
Entry contents: 2 distinct polypeptide molecules

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Assemblies

Assembly 1 (preferred)
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Assembly Name: SARS-CoV-2 cleaved Spike protein complex and Processed angiotensin-converting enzyme 2
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Multimeric state: hetero pentamer
Accessible surface area: 205957.01 Å2
Buried surface area: 47838.87 Å2
Dissociation area: 1,956.93 Å2
Dissociation energy (ΔGdiss): -9.21 kcal/mol
Dissociation entropy (TΔSdiss): 31.89 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-144663

Macromolecules

Spike glycoprotein
Chains: A, B, C
Length: 1288 amino acids
Theoretical weight: 142.54 KDa
Source organism: Severe acute respiratory syndrome coronavirus 2
Expression system: Homo sapiens
UniProt:
  • Canonical: P0DTC2 (Residues: 1-1208; Coverage: 95%)
Gene names: 2, S
Pfam:
Spike glycoprotein in PDB entry 8z4x, assembly 1, front view.
Spike glycoprotein in PDB entry 8z4x, assembly 1, side view.
Spike glycoprotein in PDB entry 8z4x, assembly 1, top view.
PDBe-KB: UniProt Coverage View: P0DTC2  
112881002003004005006007008009001,0001,1001,200
 
5001000MFVFLVLLPLVSSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFDNPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVYSSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQTLLALHRSYLTPGDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFLPFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQGVNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRAGCLIGAEHVNNSYECDIPIGAGICASYQTQTNSPRRARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTTEILPVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGFNFSQILPDPSKPSKRSFIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAGTITSGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGNCDVVIGIVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQGSGYIPEAPRDGQAYVRKDGEWVFLSTFLSGLEVLFQGPGGWSHPQFEKGGGSGGGSGGSAWSHPQFEKGGSHHHHHHHH
UniProt
P0DTC2
PRO_0000449647
PRO_0000449648
PRO_0000449649
Chains
Ligand binding sites
Interaction interfaces
Sequence conservation
Molecule details ›

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Processed angiotensin-converting enzyme 2
Chains: D, E
Length: 631 amino acids
Theoretical weight: 72.99 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9BYF1 (Residues: 1-615; Coverage: 76%)
Gene names: ACE2, UNQ868/PRO1885
Pfam: Angiotensin-converting enzyme
Angiotensin-converting enzyme 2 in PDB entry 8z4x, assembly 1, front view.
Angiotensin-converting enzyme 2 in PDB entry 8z4x, assembly 1, side view.
Angiotensin-converting enzyme 2 in PDB entry 8z4x, assembly 1, top view.
PDBe-KB: UniProt Coverage View: Q9BYF1  
163150100150200250300350400450500550600
 
200400600MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADLEVLFQGPHHHHHHHH
UniProt
Q9BYF1
Chains
Ligand binding sites
Interaction interfaces
Sequence conservation
Molecule details ›

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