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8XNF

Cryo-EM structure of SARS-CoV-2 Omicron BA.2.86 spike protein(6P) in complex with human ACE2

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
ATHR371-GLN380

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsSITE: Cleavage; by host furin => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32362314, ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616
ChainResidueDetails
BGLN689
CGLN689
DGLN689

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Cleavage; by host TMPRSS2 or CTSL => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616
ChainResidueDetails
BASP819
CASP819
DASP819

site_idSWS_FT_FI3
Number of Residues15
DetailsCARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
BASN62
CPRO1078
DASN62
DTHR124
DVAL721
DLEU805
DPRO1078
BTHR124
BVAL721
BLEU805
BPRO1078
CASN62
CTHR124
CVAL721
CLEU805

site_idSWS_FT_FI4
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
BTHR76
BTRP152
CTHR76
CTRP152
DTHR76
DTRP152

site_idSWS_FT_FI5
Number of Residues21
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
BPHE168
CLEU335
CPHE347
CSER620
CCYS661
CPHE1102
DPHE168
DTHR286
DLEU335
DPHE347
DSER620
BTHR286
DCYS661
DPHE1102
BLEU335
BPHE347
BSER620
BCYS661
BPHE1102
CPHE168
CTHR286

site_idSWS_FT_FI6
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
BPHE238
BILE713
CPHE238
CILE713
DPHE238
DILE713

site_idSWS_FT_FI7
Number of Residues3
DetailsCARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
BVAL327
CVAL327
DVAL327

site_idSWS_FT_FI8
Number of Residues3
DetailsCARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
BPHE329
CPHE329
DPHE329

site_idSWS_FT_FI9
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
BVAL607
CVAL607
DVAL607

site_idSWS_FT_FI10
Number of Residues6
DetailsCARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
ChainResidueDetails
BARG680
BSER682
CARG680
CSER682
DARG680
DSER682

site_idSWS_FT_FI11
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
BASP1138
CASP1138
DASP1138

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PDB entries from 2024-10-09

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