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5RHK

PanDDA analysis group deposition -- Crystal Structure of Zika virus NS3 Helicase in complex with Z87615031

Functional Information from GO Data
ChainGOidnamespacecontents
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue EDO A 701
ChainResidue
AARG388

site_idAC2
Number of Residues10
Detailsbinding site for residue PO4 A 702
ChainResidue
AHOH887
AHOH1028
AGLY197
AALA198
AGLY199
ALYS200
ATHR201
AARG462
AHOH826
AHOH834

site_idAC3
Number of Residues3
Detailsbinding site for residue PO4 A 703
ChainResidue
AHOH813
AHOH815
AHOH837

site_idAC4
Number of Residues4
Detailsbinding site for residue MPD A 704
ChainResidue
AALA264
ASER268
AMET536
ALYS537

site_idAC5
Number of Residues7
Detailsbinding site for residue UQM A 705
ChainResidue
ALEU488
AVAL515
AALA516
ATRP544
AHOH801
AHOH965
AHOH1013

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:0000269|PubMed:37478852
ChainResidueDetails
ALYS389

221051

PDB entries from 2024-06-12

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