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8DF5

SARS-CoV-2 Beta RBD in complex with human ACE2 and S304 Fab and S309 Fab

Functional Information from GO Data
ChainGOidnamespacecontents
E0006508biological_processproteolysis
E0008237molecular_functionmetallopeptidase activity
E0008241molecular_functionpeptidyl-dipeptidase activity
E0016020cellular_componentmembrane
F0006508biological_processproteolysis
F0008237molecular_functionmetallopeptidase activity
F0008241molecular_functionpeptidyl-dipeptidase activity
F0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
ETHR371-GLN380

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
ChainResidueDetails
HTYR201-HIS207
BTYR192-HIS198
LTYR193-HIS199
ATYR208-HIS214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
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
RASN331
RASN343
SASN331
SASN343

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU01354
ChainResidueDetails
EILE741-ILE761
FILE741-ILE761

site_idSWS_FT_FI3
Number of Residues86
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
EPHE762-PHE805
FPHE762-PHE805

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402
ChainResidueDetails
EGLU375
FGLU375

site_idSWS_FT_FI5
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
ChainResidueDetails
EHIS505
FHIS505

site_idSWS_FT_FI6
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
ChainResidueDetails
EARG169
ETRP477
ELYS481
FARG169
FTRP477
FLYS481

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:14754895
ChainResidueDetails
EARG273
EHIS345
ETYR515
FARG273
FHIS345
FTYR515

site_idSWS_FT_FI8
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
ChainResidueDetails
EHIS374
EHIS378
EGLU402
FHIS374
FHIS378
FGLU402

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498
ChainResidueDetails
ETYR781
FTYR781

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498
ChainResidueDetails
ESER783
FSER783

site_idSWS_FT_FI11
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
ChainResidueDetails
EASN53
EASN322
FASN53
FASN322

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
ChainResidueDetails
EASN90
FASN90

site_idSWS_FT_FI13
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
ChainResidueDetails
EASN103
EASN432
FASN103
FASN432

site_idSWS_FT_FI14
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337
ChainResidueDetails
EASN546
FASN546

site_idSWS_FT_FI15
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
EASN690
FASN690

site_idSWS_FT_FI16
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36876523
ChainResidueDetails
ELYS788
FLYS788

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PDB entries from 2024-07-17

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