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1QA7

CRYSTAL COMPLEX OF THE 3C PROTEINASE FROM HEPATITIS A VIRUS WITH ITS INHIBITOR AND IMPLICATIONS FOR THE POLYPROTEIN PROCESSING IN HAV

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
B0004197molecular_functioncysteine-type endopeptidase activity
B0006508biological_processproteolysis
C0004197molecular_functioncysteine-type endopeptidase activity
C0006508biological_processproteolysis
D0004197molecular_functioncysteine-type endopeptidase activity
D0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE IVF A 301
ChainResidue
AGLN15
AMET171
ACYS172
ATRP27
AVAL28
AMET29
ATHR122
AASN124
AHIS145
APRO169
AGLY170

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE IVF B 301
ChainResidue
BVAL28
BHIS44
BASN124
BPRO169
BGLY170
BMET171
BCYS172
BHOH2127
CLYS106

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE IVF C 301
ChainResidue
CTRP27
CVAL28
CMET29
CLYS147
CPRO169
CGLY170
CMET171
CCYS172
CHOH3047
CHOH3120

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE IVF D 301
ChainResidue
ALYS106
DGLN15
DVAL28
DMET29
DTHR122
DASN124
DGLY170
DMET171
DCYS172
DHOH4107

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS D 302
ChainResidue
DLYS136
DARG162
DILE198

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 303
ChainResidue
AALA70
AGLY71
AVAL73
AHOH1042
DLEU3
DARG10
DLEU129

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: For protease 3C activity => ECO:0000255|PROSITE-ProRule:PRU01222
ChainResidueDetails
AALA45
DALA45
DVAL85
DGLY173
AVAL85
AGLY173
BALA45
BVAL85
BGLY173
CALA45
CVAL85
CGLY173

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Cleavage; by protease 3C => ECO:0000269|PubMed:10559299
ChainResidueDetails
ASER1
BSER1
CSER1
DSER1

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PDB entries from 2025-06-18

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