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3KBH

Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008241molecular_functionpeptidyl-dipeptidase activity
A0016020cellular_componentmembrane
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008241molecular_functionpeptidyl-dipeptidase activity
B0016020cellular_componentmembrane
C0006508biological_processproteolysis
C0008237molecular_functionmetallopeptidase activity
C0008241molecular_functionpeptidyl-dipeptidase activity
C0016020cellular_componentmembrane
D0006508biological_processproteolysis
D0008237molecular_functionmetallopeptidase activity
D0008241molecular_functionpeptidyl-dipeptidase activity
D0016020cellular_componentmembrane
E0019064biological_processfusion of virus membrane with host plasma membrane
F0019064biological_processfusion of virus membrane with host plasma membrane
G0019064biological_processfusion of virus membrane with host plasma membrane
H0019064biological_processfusion of virus membrane with host plasma membrane
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 Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000269|PubMed:19901337, ECO:0000269|PubMed:27617430
ChainResidueDetails
EASN486
EASN512
FASN486
FASN512
GASN486
GASN512
HASN486
HASN512

site_idSWS_FT_FI2
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc) asparagine; by host => ECO:0000269|PubMed:27617430
ChainResidueDetails
EASN506
FASN506
GASN506
HASN506

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
ChainResidueDetails
AARG169
DARG169
DTRP477
DLYS481
ATRP477
ALYS481
BARG169
BTRP477
BLYS481
CARG169
CTRP477
CLYS481

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:14754895
ChainResidueDetails
AARG273
DARG273
DHIS345
DTYR515
AHIS345
ATYR515
BARG273
BHIS345
BTYR515
CARG273
CHIS345
CTYR515

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
ChainResidueDetails
AHIS374
DHIS374
DHIS378
DGLU402
AHIS378
AGLU402
BHIS374
BHIS378
BGLU402
CHIS374
CHIS378
CGLU402

site_idSWS_FT_FI6
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
ChainResidueDetails
AASN53
AASN322
BASN53
BASN322
CASN53
CASN322
DASN53
DASN322

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
ChainResidueDetails
AASN90
BASN90
CASN90
DASN90

site_idSWS_FT_FI8
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
ChainResidueDetails
AASN103
AASN432
BASN103
BASN432
CASN103
CASN432
DASN103
DASN432

site_idSWS_FT_FI9
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337
ChainResidueDetails
AASN546
BASN546
CASN546
DASN546

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PDB entries from 2025-06-11

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