6MVO: HCV NS5B 1A Y316

HCV NS5B 1A Y316 bound to Compound 49. Determined by X-ray diffraction at 1.95 Å resolution. Released 4 Sept 2019.

Method
X-ray diffraction
Resolution
1.95 Å
Organism
Hepacivirus C
Chains
2
Atoms
9,065
Mol. weight
125.81 kDa
Ligands
K4P
Released
4 Sept 2019

Explore 6MVO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6MVO contains 85 α-helices and 56 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 43 helices, 29 β-strands

ElementResiduesLengthSheet
β-strand211
β-strand4-632
α-helix9-113
β-strand2013
α-helix21-233
α-helix25-284
α-helix34-363
β-strand37-3933
α-helix42-443
α-helix45-528
β-strand5511
α-helix62-7514
β-strand7914
α-helix82-843
α-helix85-906
α-helix96-994
α-helix105-1095
α-helix113-12816
α-helix133-1353
β-strand136-14052
β-strand144-14633
β-strand14815
α-helix149-1513
β-strand15315
α-helix155-1584
β-strand159-16242
α-helix165-18723
α-helix188-1903
β-strand19116
α-helix192-1943
α-helix197-21014
β-strand214-22076
β-strand22117
α-helix224-2274
α-helix230-24011
β-strand24414
α-helix247-25610
α-helix257-2615
β-strand264-26742
β-strand273-27752
α-helix287-30519
β-strand309-31686
β-strand319-32576
α-helix329-34517
β-strand35017
β-strand35716
α-helix360-3623
β-strand36518
β-strand368-37478
β-strand380-38678
α-helix389-40012
β-strand405-40629
α-helix408-4147
α-helix419-4202
α-helix421-4266
α-helix427-4359
β-strand443-44759
β-strand450-45459
α-helix456-4583
α-helix459-4679
α-helix469-4724
β-strand47518
α-helix479-49214
α-helix494-4963
α-helix497-51418
α-helix516-5205
α-helix521-5255
α-helix527-5293
α-helix537-5393
α-helix540-5445
α-helix548-5514
β-strand56119
Chain B: 42 helices, 27 β-strands
ElementResiduesLengthSheet
β-strand2110
β-strand4-6311
α-helix9-113
β-strand20112
α-helix21-233
α-helix25-284
α-helix34-363
β-strand37-39312
α-helix42-443
α-helix45-528
β-strand55110
α-helix62-7514
β-strand79113
α-helix82-843
α-helix85-906
α-helix97-993
α-helix105-1095
α-helix113-12816
α-helix133-1353
β-strand136-140511
β-strand144-146312
α-helix149-1513
α-helix154-1585
β-strand159-162411
α-helix165-18723
α-helix188-1903
β-strand191114
α-helix192-1943
α-helix197-21014
β-strand214-220714
β-strand221115
α-helix224-2274
α-helix230-24011
β-strand244113
α-helix247-25610
α-helix257-2615
β-strand264-267411
β-strand273-277511
α-helix287-30519
β-strand309-316814
β-strand319-325714
α-helix329-34517
β-strand350115
β-strand357114
α-helix360-3623
β-strand365116
β-strand368-374716
β-strand380-386716
α-helix389-40012
β-strand405-406217
α-helix408-4147
α-helix419-4202
α-helix421-4266
α-helix427-4359
β-strand443-447517
β-strand450-454517
α-helix456-4583
α-helix459-4679
α-helix469-4724
β-strand475116
α-helix479-49214
α-helix494-4963
α-helix497-51418
α-helix516-5205
α-helix521-5255
α-helix527-5293
α-helix537-5393
α-helix540-5445
β-strand561117

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RNA-directed RNA polymeraseA, Bprotein562Hepacivirus CP26664 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6MVO_1 RNA-directed RNA polymerase (chains A, B)
SMSYSWTGALVTPCAAEEQKLPINALSNSLLRHHNLVYSTTSRSACQRQKKVTFDRLQVL
DSHYQDVLKEVKAAASKVKANLLSVEEACSLTPPHSAKSKYGYGAKDVRSHASRAVAHIN
SVWKDLLEDSVTPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVS
KLPLAVMGSSYGFQYSPGQRVEFLVQAWKSKKTPMGFSYDTRCFDSTVTESDIRTEEAIY
QCCDLDPQARVAIKSLTERLYVGGPLTNSRGENCGYRRCRASGVLTTSCGNTLTCYIKAR
AACRAAGLQDCTMLVYGDDLVVICESAGVQEDAASLRAFTEAMTRYSAPPGDPPQPEYDL
ELITSCSSNVSVAHDGAGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMFAPTLW
ARMILMTHFFSVLIARDQLEQALDCEIYGACYSIEPLDLPPIIQRLHGLSAFSLHSYSPG
EINRVAACLRKLGVPPLRAWRHRARSVRARLLSRGGRAAICGKYLFNWAVRTKLKLTPIA
AAGQLALSGWFTAGYSGGDIYH

Ligands and cofactors

IDNameFormulaCopies
K4P6-[(7-chloro-1-hydroxy-1,3-dihydro-2,1-benzoxaborol-5-yl)(methylsulfonyl)amino]…C27 H23 B Cl F N2 O6 S2

Water and common crystallization additives (SO4) are not listed.

Primary citation

Design of N-Benzoxaborole Benzofuran GSK8175-Optimization of Human Pharmacokinetics Inspired by Metabolites of a Failed Clinical HCV Inhibitor. Chong, P.Y., Shotwell, J.B., Miller, J. et al. J Med Chem (2019) 62:3254-3267. DOI 10.1021/acs.jmedchem.8b01719 · PubMed

Other PDB entries of the same protein (UniProt P26664 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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