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3KQU

Three Conformational Snapshots of the Hepatitis C Virus NS3 Helicase Reveal a Ratchet Translocation Mechanism

Functional Information from GO Data
ChainGOidnamespacecontents
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
B0004386molecular_functionhelicase activity
B0005524molecular_functionATP binding
C0004386molecular_functionhelicase activity
C0005524molecular_functionATP binding
D0004386molecular_functionhelicase activity
D0005524molecular_functionATP binding
E0004386molecular_functionhelicase activity
E0005524molecular_functionATP binding
F0004386molecular_functionhelicase activity
F0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BEF A 1
ChainResidue
AADP2
AARG467
AHOH626
AHOH627
AHOH628
AMN3
AHOH4
ATHR206
AGLY207
ALYS210
AGLU291
AALA323
AARG464

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP A 2
ChainResidue
ABEF1
AMN3
AHOH4
AHOH5
AGLY207
ASER208
AGLY209
ALYS210
ASER211
ATHR212
AGLY237
ATYR241
ATHR419
AARG467
AGLY468
AHOH628

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 3
ChainResidue
ABEF1
AADP2
AHOH4
ASER211
AASP290
AGLU291
AHOH628

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE BEF B 1
ChainResidue
BADP2
BMN3
BHOH6
BHOH7
BHOH8
BHOH9
BTHR206
BLYS210
BGLU291
BALA323
BARG464
BARG467

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ADP B 2
ChainResidue
BBEF1
BMN3
BHOH8
BHOH9
BHOH10
BGLY207
BSER208
BGLY209
BLYS210
BSER211
BTHR212
BGLY237
BTYR241
BTHR419
BARG467
BGLY468
BHOH633
BHOH662

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN B 3
ChainResidue
BBEF1
BADP2
BHOH8
BHOH9
BSER211
BASP290
BGLU291

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BEF C 1
ChainResidue
CADP2
CMN3
CHOH11
CHOH12
CHOH13
CHOH14
CTHR206
CGLY207
CLYS210
CGLU291
CALA323
CARG464
CARG467

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP C 2
ChainResidue
CTHR419
CARG467
CGLY468
CBEF1
CMN3
CHOH13
CHOH14
CHOH15
CGLY207
CSER208
CGLY209
CLYS210
CSER211
CTHR212
CGLY237
CTYR241

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN C 3
ChainResidue
CBEF1
CADP2
CHOH13
CHOH14
CSER211
CASP290
CGLU291

site_idBC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BEF D 1
ChainResidue
DADP2
DMN3
DHOH16
DHOH17
DHOH18
DHOH19
DTHR206
DGLY207
DLYS210
DGLU291
DALA323
DARG464
DARG467

site_idBC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP D 2
ChainResidue
DBEF1
DMN3
DHOH18
DHOH19
DHOH20
DGLY207
DSER208
DGLY209
DLYS210
DSER211
DTHR212
DGLY237
DTYR241
DTHR419
DARG467
DGLY468

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN D 3
ChainResidue
DBEF1
DADP2
DHOH18
DHOH19
DSER211
DASP290
DGLU291

site_idBC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BEF E 1
ChainResidue
EADP2
EMN3
EHOH21
EHOH22
EHOH23
EHOH24
ETHR206
EGLY207
ELYS210
EGLU291
EALA323
EARG464
EARG467

site_idBC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP E 2
ChainResidue
EBEF1
EMN3
EHOH23
EHOH24
EHOH25
EGLY207
ESER208
EGLY209
ELYS210
ESER211
ETHR212
EGLY237
ETYR241
ETHR419
EARG467
EGLY468

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN E 3
ChainResidue
EBEF1
EADP2
EHOH23
EHOH24
ESER211
EASP290
EGLU291

site_idBC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BEF F 1
ChainResidue
FADP2
FMN3
FHOH26
FHOH27
FHOH28
FHOH29
FTHR206
FGLY207
FLYS210
FGLU291
FALA323
FARG464
FARG467

site_idBC8
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ADP F 2
ChainResidue
FBEF1
FMN3
FHOH28
FHOH29
FHOH30
FGLY207
FSER208
FGLY209
FLYS210
FSER211
FTHR212
FGLY237
FTYR241
FTHR419
FARG467
FGLY468
FHOH642

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN F 3
ChainResidue
FBEF1
FADP2
FHOH28
FHOH29
FSER211
FASP290
FGLU291

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
ChainResidueDetails
AALA204
BALA204
CALA204
DALA204
EALA204
FALA204

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:20080715
ChainResidueDetails
ASER211
EGLU291
FSER211
FGLU291
AGLU291
BSER211
BGLU291
CSER211
CGLU291
DSER211
DGLU291
ESER211

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PDB entries from 2024-10-16

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