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2WHX

A second conformation of the NS3 protease-helicase from dengue virus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003724molecular_functionRNA helicase activity
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP A 1619
ChainResidue
AGLY196
AHOH2133
AHOH2134
AHOH2136
AHOH2137
AALA197
AGLY198
ALYS199
ATHR200
ALYS201
AASN329
AARG463
AMN1620

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 1620
ChainResidue
ATHR200
AGLU285
AADP1619
AHOH2135
AHOH2136
AHOH2137

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1621
ChainResidue
ALYS199
AALA316
AGLN456
AHOH2091

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1622
ChainResidue
AILE365
AARG387
ATHR408

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU00860
ChainResidueDetails
AHIS51
AASP75
ASER135

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
ChainResidueDetails
ALEU193

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Involved in NS3 ATPase and RTPase activities => ECO:0000250|UniProtKB:P14335
ChainResidueDetails
AARG457
AARG460

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P29990
ChainResidueDetails
ALYS618

219140

PDB entries from 2024-05-01

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