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8AQW

BA.4/5 SARS-CoV-2 Spike bound to mouse ACE2 (local)

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008241molecular_functionpeptidyl-dipeptidase activity
A0016020cellular_componentmembrane
B0016020cellular_componentmembrane
B0019031cellular_componentviral envelope
B0019064biological_processfusion of virus membrane with host plasma membrane
B0039654biological_processfusion of virus membrane with host endosome membrane
B0046813biological_processreceptor-mediated virion attachment to host cell
B0055036cellular_componentvirion membrane
B0075509biological_processendocytosis involved in viral entry into host cell
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
ATHR371-GLN380

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCSVVH
ChainResidueDetails
ATYR834-HIS840

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. ATSTdyNsRLWAWEG
ChainResidueDetails
AALA153-GLY167

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
AGLU375

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
AHIS505

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
AARG169
AHIS374
AHIS378
AGLU402
ATRP477
ALYS481

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9BYF1
ChainResidueDetails
BLEU806
BPRO1079
AARG273
AHIS345
ATYR515

site_idSWS_FT_FI5
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN536
AASN53
AASN546

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17330941
ChainResidueDetails
AASN708
BASP287
BCYS336
BALA348
BPRO621
BCYS662
BPHE1103

site_idSWS_FT_FI7
Number of Residues2
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
BGLN239
BILE714

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
BARG328

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
BPRO330

site_idSWS_FT_FI10
Number of Residues1
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
BVAL608

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
ChainResidueDetails
BHIS681
BSER683

site_idSWS_FT_FI12
Number of Residues1
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
BASP1139

221051

PDB entries from 2024-06-12

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