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5YVW

Crystal structure of full length NS3 protein (eD4NS2BNS3) from DENV4 in closed conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0044423cellular_componentvirion component
B0003723molecular_functionRNA binding
B0003724molecular_functionRNA helicase activity
B0004386molecular_functionhelicase activity
B0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue EPE B 701
ChainResidue
BLEU193
BGLY414
BASN416
BGLN456
BARG460
BARG463
BHIS194
BPRO195
BGLY196
BALA197
BGLY198
BLYS199
BGLU285
BALA316

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
BHIS51
BASP75
BALA135

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
ChainResidueDetails
BLEU193

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Involved in NS3 ATPase and RTPase activities => ECO:0000250|UniProtKB:P14335
ChainResidueDetails
BARG457
BARG460

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P29990
ChainResidueDetails
BLYS618

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by host => ECO:0000250|UniProtKB:Q32ZE1
ChainResidueDetails
BLYS388

222415

PDB entries from 2024-07-10

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