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5GQ1

Crystal structure of 2C helicase from enterovirus 71 (EV71)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003724molecular_functionRNA helicase activity
A0016887molecular_functionATP hydrolysis activity
B0003723molecular_functionRNA binding
B0003724molecular_functionRNA helicase activity
B0016887molecular_functionATP hydrolysis activity
C0003723molecular_functionRNA binding
C0003724molecular_functionRNA helicase activity
C0016887molecular_functionATP hydrolysis activity
D0003723molecular_functionRNA binding
D0003724molecular_functionRNA helicase activity
D0016887molecular_functionATP hydrolysis activity
E0003723molecular_functionRNA binding
E0003724molecular_functionRNA helicase activity
E0016887molecular_functionATP hydrolysis activity
F0003723molecular_functionRNA binding
F0003724molecular_functionRNA helicase activity
F0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
ACYS270
ACYS281
ASER282
ACYS286
AHOH511

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BCYS270
BCYS281
BSER282
BCYS286

site_idAC3
Number of Residues4
Detailsbinding site for residue PO4 B 402
ChainResidue
BGLY132
BGLY134
BLYS135
BSER136

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN C 401
ChainResidue
CCYS270
CCYS281
CSER282
CCYS286

site_idAC5
Number of Residues5
Detailsbinding site for residue ZN D 401
ChainResidue
DCYS270
DCYS281
DSER282
DCYS286
DLYS288

site_idAC6
Number of Residues3
Detailsbinding site for residue PO4 D 402
ChainResidue
DGLY134
DLYS135
DSER136

site_idAC7
Number of Residues3
Detailsbinding site for residue ZN E 401
ChainResidue
ECYS281
ESER282
ECYS286

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN F 401
ChainResidue
FCYS270
FCYS281
FSER282
FCYS286

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues96
DetailsZN_FING: C4-type; degenerate => ECO:0000269|DOI:10.1126/sciadv.1602573
ChainResidueDetails
ACYS270-CYS286
BCYS270-CYS286
CCYS270-CYS286
DCYS270-CYS286
ECYS270-CYS286
FCYS270-CYS286

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00551
ChainResidueDetails
AGLY129
BGLY129
CGLY129
DGLY129
EGLY129
FGLY129

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|DOI:10.1126/sciadv.1602573
ChainResidueDetails
ACYS270
CCYS281
CSER282
CCYS286
DCYS270
DCYS281
DSER282
DCYS286
ECYS270
ECYS281
ESER282
ACYS281
ECYS286
FCYS270
FCYS281
FSER282
FCYS286
ASER282
ACYS286
BCYS270
BCYS281
BSER282
BCYS286
CCYS270

site_idSWS_FT_FI4
Number of Residues6
DetailsSITE: Cleavage; by protease 3C => ECO:0000250|UniProtKB:P03301
ChainResidueDetails
AGLN329
BGLN329
CGLN329
DGLN329
EGLN329
FGLN329

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PDB entries from 2024-05-01

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