3EB8: VirA

VirA. Determined by X-ray diffraction at 2.4 Å resolution. Released 30 Sept 2008.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Shigella flexneri
Chains
2
Atoms
5,371
Mol. weight
79.75 kDa
Released
30 Sept 2008

Explore 3EB8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3EB8 contains 34 α-helices and 32 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: 17 helices, 16 β-strands

ElementResiduesLengthSheet
α-helix54-6310
β-strand66-6721
α-helix73-742
β-strand77-8371
β-strand86-9381
β-strand96-10381
β-strand108-11141
α-helix112-1132
α-helix114-12310
β-strand128-12922
β-strand136-13942
α-helix152-1609
β-strand163-16532
β-strand17113
α-helix172-1743
α-helix182-19110
α-helix193-1953
β-strand199-20242
β-strand205-20622
α-helix207-2082
α-helix209-21810
α-helix231-2355
α-helix236-24611
α-helix252-26312
α-helix268-2769
β-strand28613
α-helix287-30721
β-strand316-325102
β-strand342-354132
β-strand357-369132
α-helix377-3837
α-helix386-3883
β-strand390-39892
Chain B: 17 helices, 16 β-strands
ElementResiduesLengthSheet
α-helix57-604
β-strand66-6724
α-helix73-742
β-strand77-8374
β-strand86-9384
β-strand96-10384
β-strand108-11144
α-helix112-1132
α-helix114-12310
β-strand128-12925
β-strand136-13945
α-helix152-1609
β-strand163-16535
β-strand17116
α-helix172-1743
α-helix182-19110
α-helix193-1953
β-strand199-20245
β-strand205-20625
α-helix207-2082
α-helix209-21810
α-helix229-2357
α-helix236-24611
α-helix252-26312
α-helix268-2769
β-strand28616
α-helix287-30721
β-strand316-325105
β-strand342-354135
β-strand357-369135
α-helix377-3837
α-helix386-3883
β-strand390-39895

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cysteine protease-like virAA, Bprotein358Shigella flexneriQ7BU69 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3EB8_1 Cysteine protease-like virA (chains A, B)
GSIYSPHETLAEKHSEKKLMDSFSPSLSQDKMDGEFAHANIDGISIRLCLNKGICSVFYL
DGDKIQSTQLSSKEYNNLLSSLPPKQFNLGKVHTITAPVSGNFKTHKPAPEVIETAINCC
TSIIPNDDYFHVKDTDFNSVWHDIYRDIRASDSNSTKIYFNNIEIPLKLIADLINELGIN
EFIDSKKELQMLSYNQVNKIINSNFPQQDLCFQTEKLLFTSLFQDPAFISALTSAFWQSL
HITSSSVEHIYAQIMSENIENRLNFMPEQRVINNCGHIIKINAVVPKNDTAISASGGRAY
EVSSSILPSHITCNGVGINKIETSYLVHAGTLPSSEGLRNAIPPESRQVSFAIISPDV

Primary citation

Structural and functional studies indicate that Shigella VirA is not a protease and does not directly destabilize microtubules. Germane, K.L., Ohi, R., Goldberg, M.B. et al. Biochemistry (2008) 47:10241-10243. DOI 10.1021/bi801533k · PubMed

Other PDB entries of the same protein (UniProt Q7BU69 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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