5NJV: Flavivirus NS5 domain

Flavivirus NS5 domain. Determined by X-ray diffraction at 2.0 Å resolution. Released 24 Jan 2018.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Zika virus (strain Mr 766)
Chains
4
Atoms
8,667
Mol. weight
118.05 kDa
Ligands
SAM
Released
24 Jan 2018

Explore 5NJV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NJV contains 54 α-helices and 42 β-strands across 4 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: 13 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix8-1811
α-helix21-277
β-strand33-3531
α-helix38-469
α-helix58-6710
β-strand75-8062
α-helix86-927
β-strand97-10372
α-helix121-1233
β-strand124-12742
α-helix132-1343
α-helix136-1372
β-strand142-14542
α-helix154-17219
β-strand178-18362
α-helix189-20214
β-strand205-20732
β-strand219-22242
α-helix229-24517
α-helix247-2515
β-strand252-25431
α-helix255-2573
Chain B: 14 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix8-1811
α-helix21-299
β-strand33-3533
α-helix38-469
α-helix58-669
β-strand75-8064
α-helix86-927
β-strand97-10374
α-helix111-1144
α-helix121-1233
β-strand124-12744
α-helix136-1372
β-strand142-14544
α-helix154-17219
β-strand178-18364
α-helix189-20214
β-strand205-20734
β-strand219-22244
α-helix229-24517
α-helix247-2482
α-helix250-2512
β-strand252-25433
α-helix255-2573
Chain C: 13 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix8-169
β-strand2015
α-helix21-288
β-strand33-3536
α-helix38-414
β-strand5317
α-helix58-6710
β-strand75-8068
α-helix86-916
β-strand97-10378
α-helix121-1233
β-strand124-12748
α-helix132-1343
α-helix136-1372
β-strand142-14548
α-helix154-17219
β-strand178-18368
α-helix189-20214
β-strand205-20738
β-strand219-22248
α-helix229-24214
α-helix249-2513
β-strand252-25436
α-helix255-2573
β-strand25817
Chain D: 14 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix8-1811
β-strand2015
α-helix21-277
β-strand33-3649
α-helix38-414
β-strand53110
α-helix58-6710
β-strand75-80611
α-helix86-916
β-strand97-103711
α-helix111-1144
α-helix121-1233
β-strand124-127411
α-helix132-1343
α-helix136-1372
β-strand142-145411
α-helix154-17219
β-strand178-183611
α-helix189-20214
β-strand205-207311
β-strand219-222411
α-helix229-24517
α-helix247-2515
β-strand252-25549
α-helix256-2572
β-strand258110

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
NS5A, B, C, Dprotein262Zika virus (strain Mr 766)A0A024B7W1 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>5NJV_1 NS5 (chains A, B, C, D)
TGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLR
WLVDRGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPVLVQSYGWNI
VRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKV
LCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGR
MDGPRRPVKYEEDVNLGSGTRA

Ligands and cofactors

IDNameFormulaCopies
SAMS-adenosylmethionineC15 H22 N6 O5 S4

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

Primary citation

The structure of the binary methyltransferase-SAH complex from Zika virus reveals a novel conformation for the mechanism of mRNA capping. Chatrin, C., Talapatra, S.K., Canard, B. et al. Oncotarget (2018) 9:3160-3171. DOI 10.18632/oncotarget.23223 · PubMed

Other PDB entries of the same protein (UniProt A0A024B7W1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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