Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5RHG

PanDDA analysis group deposition -- Crystal Structure of Zika virus NS3 Helicase in complex with Z235341991

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 Residues9
Detailsbinding site for residue PO4 A 702
ChainResidue
AHOH987
AGLY197
AALA198
AGLY199
ALYS200
ATHR201
AARG462
AHOH816
AHOH826

site_idAC3
Number of Residues4
Detailsbinding site for residue PO4 A 703
ChainResidue
AARG598
AHOH813
AHOH825
AHOH841

site_idAC4
Number of Residues6
Detailsbinding site for residue NY7 A 704
ChainResidue
AALA264
ATHR265
ASER268
ALYS537
AASP540
APO4706

site_idAC5
Number of Residues9
Detailsbinding site for residue NY7 A 705
ChainResidue
AGLY299
ASER302
ATHR303
AGLU306
ASER506
ALEU507
ATYR508
AARG509
AHOH894

site_idAC6
Number of Residues3
Detailsbinding site for residue PO4 A 706
ChainResidue
ALYS537
ANY7704
AHOH925

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

221371

PDB entries from 2024-06-19

PDB statisticsPDBj update infoContact PDBjnumon