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5MZ4

Crystal Structure of full-lengh CSFV NS3/4A

Replaces:  5LKL
Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
B0004252molecular_functionserine-type endopeptidase activity
B0004386molecular_functionhelicase activity
B0005524molecular_functionATP binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU00868
ChainResidueDetails
AHIS110
AASP147
AALA204
BHIS110
BASP147
BALA204

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
ChainResidueDetails
ALEU267
BLEU267

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by serine protease NS3 => ECO:0000250
ChainResidueDetails
ALEU724
BLEU723

site_idSWS_FT_FI4
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255
ChainResidueDetails
AASN165
AASN586
AASN669
BASN165
BASN585
BASN668

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PDB entries from 2024-07-17

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