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6L50

Crystal structure of Zika NS2B-NS3 protease with compound 16

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0044423cellular_componentvirion component
B0003723molecular_functionRNA binding
B0003724molecular_functionRNA helicase activity
B0005524molecular_functionATP binding
C0004252molecular_functionserine-type endopeptidase activity
C0044423cellular_componentvirion component
D0003723molecular_functionRNA binding
D0003724molecular_functionRNA helicase activity
D0005524molecular_functionATP binding
E0004252molecular_functionserine-type endopeptidase activity
E0044423cellular_componentvirion component
F0003723molecular_functionRNA binding
F0003724molecular_functionRNA helicase activity
F0005524molecular_functionATP binding
G0004252molecular_functionserine-type endopeptidase activity
G0044423cellular_componentvirion component
H0003723molecular_functionRNA binding
H0003724molecular_functionRNA helicase activity
H0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue E60 H 201
ChainResidue
HTYR130
HPRO131
HSER135
HGLY151
HTYR161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU00860
ChainResidueDetails
BHIS51
BASP75
DHIS51
DASP75
FHIS51
FASP75
HHIS51
HASP75

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU00860, ECO:0000269|PubMed:29526431
ChainResidueDetails
BSER135
DSER135
FSER135
HSER135

226707

PDB entries from 2024-10-30

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