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6S0J

Structure of Zika virus NS3 helicase in complex with ADP-MgF3(H2O)-

Functional Information from GO Data
ChainGOidnamespacecontents
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue KQB A 701
ChainResidue
APRO196
AHOH817
AHOH832
AHOH857
AHOH871
AHOH967
AGLY197
ALYS200
AGLU286
AGLY415
AARG459
AARG462
AMG702
AADP703

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 702
ChainResidue
ATHR201
AKQB701
AADP703
AHOH817
AHOH871
AHOH967

site_idAC3
Number of Residues18
Detailsbinding site for residue ADP A 703
ChainResidue
AGLY197
AALA198
AGLY199
ALYS200
ATHR201
AARG202
AASN330
AASN417
AARG462
AKQB701
AMG702
AHOH817
AHOH823
AHOH841
AHOH871
AHOH912
AHOH924
AHOH1041

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
ChainResidueDetails
ALEU194

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Involved in NS3 ATPase and RTPase activities => ECO:0000250|UniProtKB:P14335
ChainResidueDetails
AARG456
AARG459

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage; by autolysis => ECO:0000250|UniProtKB:P06935
ChainResidueDetails
AARG617

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by host => ECO:0000250|UniProtKB:Q32ZE1
ChainResidueDetails
ALYS389

222624

PDB entries from 2024-07-17

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