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8YOY

Structure of HKU1A RBD with TMPRSS2

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
ChainResidueDetails
BVAL292-CYS297

site_idPS01209
Number of Residues23
DetailsLDLRA_1 LDL-receptor class A (LDLRA) domain signature. CInpsnw.CDgvsHCpgg.EDEnr...C
ChainResidueDetails
BCYS126-CYS148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:11245484, ECO:0000269|PubMed:38964326
ChainResidueDetails
BHIS296
AASN433
AASN454
AASN470
AASN564
AASN666

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:38964326
ChainResidueDetails
BASP345
BALA441

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:37990007, ECO:0000269|PubMed:38964326, ECO:0007744|PDB:7XYD, ECO:0007744|PDB:7Y0E, ECO:0007744|PDB:7Y0F, ECO:0007744|PDB:8HD8, ECO:0007744|PDB:8S0L
ChainResidueDetails
BASN131
BASP134
BVAL136
BASP144
BGLU145

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:11245484, ECO:0000269|PubMed:38964328
ChainResidueDetails
BARG255

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:37990007, ECO:0000269|PubMed:38964326, ECO:0007744|PDB:7XYD, ECO:0007744|PDB:7Y0E, ECO:0007744|PDB:7Y0F, ECO:0007744|PDB:8HD8, ECO:0007744|PDB:8S0L, ECO:0007744|PDB:8S0M
ChainResidueDetails
BASN213

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN249

237992

PDB entries from 2025-06-25

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