4XC5: T1L reovirus attachment protein SIGMA1

Crystal structure of the T1L reovirus attachment protein SIGMA1. Determined by X-ray diffraction at 2.2 Å resolution. Released 1 Apr 2015.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Mammalian orthoreovirus 1 Lang
Chains
3
Atoms
3,951
Mol. weight
74.94 kDa
Ligands
MG
Released
1 Apr 2015

Explore 4XC5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4XC5 contains 9 α-helices and 42 β-strands across 3 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.

Chains A, B and C: 3 helices, 14 β-strands

ElementResiduesLengthSheet
β-strand310-31121
β-strand315-31842
β-strand323-32642
α-helix328-3314
β-strand333-345133
β-strand348-361143
β-strand364-36963
β-strand372-37543
β-strand381-38663
β-strand39113
α-helix3921
α-helix397-4004
β-strand410-420113
β-strand423-437153
β-strand440-44893
β-strand455-45843
β-strand461-46663

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Outer capsid protein sigma-1A, B, Cprotein218Mammalian orthoreovirus 1 LangP04506
Sequence of entity 1 (A, B, C), FASTA
>4XC5_1 Outer capsid protein sigma-1 (chains A, B, C)
HHHHHHGSSNSGKQIEDKIEEILSKIYHIENEIARIKKLIGEGSGRGVLNQGVTSLPTYR
YPLELDTANNRVQVADRFGMRTGTWTGQLQYQHPQLSWRANVTLNLMKVDDWLVLSFSQM
TTNSIMADGKFVINFVSGLSSGWQTGDTEPSSTIDPLSTTFAAVQFLNNGQRIDAFRIMG
VSEWTDGELEIKNYGGTYTGHTQVYWAPWTIMYPCNVR

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg3

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

Primary citation

Structure of Serotype 1 Reovirus Attachment Protein sigma 1 in Complex with Junctional Adhesion Molecule A Reveals a Conserved Serotype-Independent Binding Epitope. Stettner, E., Dietrich, M.H., Reiss, K. et al. J Virol (2015) 89:6136-6140. DOI 10.1128/JVI.00433-15 · PubMed

Other PDB entries of the same protein (UniProt P04506), best resolution first:

Browse structure collections

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