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7L7F

Cryo-EM structure of human ACE2 receptor bound to protein encoded by vaccine candidate BNT162b1

Functional Information from GO Data
ChainGOidnamespacecontents
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008241molecular_functionpeptidyl-dipeptidase activity
B0016020cellular_componentmembrane
D0006508biological_processproteolysis
D0008237molecular_functionmetallopeptidase activity
D0008241molecular_functionpeptidyl-dipeptidase activity
D0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
ChainResidueDetails
BTHR371-GLN380

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
ESER323
FSER323

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
ECYS325
FCYS325

site_idSWS_FT_FI3
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
EASN331
EASN343
FASN331
FASN343

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
BGLU375
DGLU375

site_idSWS_FT_FI5
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
ChainResidueDetails
BHIS505
DHIS505

site_idSWS_FT_FI6
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
ChainResidueDetails
BARG169
BTRP477
BLYS481
DARG169
DTRP477
DLYS481

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:14754895
ChainResidueDetails
BARG273
BHIS345
BTYR515
DARG273
DHIS345
DTYR515

site_idSWS_FT_FI8
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
ChainResidueDetails
BHIS374
BHIS378
BGLU402
DHIS374
DHIS378
DGLU402

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498
ChainResidueDetails
BTYR781
DTYR781

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498
ChainResidueDetails
BSER783
DSER783

site_idSWS_FT_FI11
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
ChainResidueDetails
BASN53
BASN322
DASN53
DASN322

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
BASN90
DASN90

site_idSWS_FT_FI13
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
ChainResidueDetails
BASN103
BASN432
DASN103
DASN432

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
BASN546
DASN546

site_idSWS_FT_FI15
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN690
DASN690

site_idSWS_FT_FI16
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36876523
ChainResidueDetails
BLYS788
DLYS788

223790

PDB entries from 2024-08-14

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