VirA. Determined by X-ray diffraction at 2.4 Å resolution. Released 30 Sept 2008.
Explore 3EB8 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 54-63 | 10 | |
| β-strand | 66-67 | 2 | 1 |
| α-helix | 73-74 | 2 | |
| β-strand | 77-83 | 7 | 1 |
| β-strand | 86-93 | 8 | 1 |
| β-strand | 96-103 | 8 | 1 |
| β-strand | 108-111 | 4 | 1 |
| α-helix | 112-113 | 2 | |
| α-helix | 114-123 | 10 | |
| β-strand | 128-129 | 2 | 2 |
| β-strand | 136-139 | 4 | 2 |
| α-helix | 152-160 | 9 | |
| β-strand | 163-165 | 3 | 2 |
| β-strand | 171 | 1 | 3 |
| α-helix | 172-174 | 3 | |
| α-helix | 182-191 | 10 | |
| α-helix | 193-195 | 3 | |
| β-strand | 199-202 | 4 | 2 |
| β-strand | 205-206 | 2 | 2 |
| α-helix | 207-208 | 2 | |
| α-helix | 209-218 | 10 | |
| α-helix | 231-235 | 5 | |
| α-helix | 236-246 | 11 | |
| α-helix | 252-263 | 12 | |
| α-helix | 268-276 | 9 | |
| β-strand | 286 | 1 | 3 |
| α-helix | 287-307 | 21 | |
| β-strand | 316-325 | 10 | 2 |
| β-strand | 342-354 | 13 | 2 |
| β-strand | 357-369 | 13 | 2 |
| α-helix | 377-383 | 7 | |
| α-helix | 386-388 | 3 | |
| β-strand | 390-398 | 9 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 57-60 | 4 | |
| β-strand | 66-67 | 2 | 4 |
| α-helix | 73-74 | 2 | |
| β-strand | 77-83 | 7 | 4 |
| β-strand | 86-93 | 8 | 4 |
| β-strand | 96-103 | 8 | 4 |
| β-strand | 108-111 | 4 | 4 |
| α-helix | 112-113 | 2 | |
| α-helix | 114-123 | 10 | |
| β-strand | 128-129 | 2 | 5 |
| β-strand | 136-139 | 4 | 5 |
| α-helix | 152-160 | 9 | |
| β-strand | 163-165 | 3 | 5 |
| β-strand | 171 | 1 | 6 |
| α-helix | 172-174 | 3 | |
| α-helix | 182-191 | 10 | |
| α-helix | 193-195 | 3 | |
| β-strand | 199-202 | 4 | 5 |
| β-strand | 205-206 | 2 | 5 |
| α-helix | 207-208 | 2 | |
| α-helix | 209-218 | 10 | |
| α-helix | 229-235 | 7 | |
| α-helix | 236-246 | 11 | |
| α-helix | 252-263 | 12 | |
| α-helix | 268-276 | 9 | |
| β-strand | 286 | 1 | 6 |
| α-helix | 287-307 | 21 | |
| β-strand | 316-325 | 10 | 5 |
| β-strand | 342-354 | 13 | 5 |
| β-strand | 357-369 | 13 | 5 |
| α-helix | 377-383 | 7 | |
| α-helix | 386-388 | 3 | |
| β-strand | 390-398 | 9 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cysteine protease-like virA | A, B | protein | 358 | Shigella flexneri | Q7BU69 (AlphaFold model) |
>3EB8_1 Cysteine protease-like virA (chains A, B) GSIYSPHETLAEKHSEKKLMDSFSPSLSQDKMDGEFAHANIDGISIRLCLNKGICSVFYL DGDKIQSTQLSSKEYNNLLSSLPPKQFNLGKVHTITAPVSGNFKTHKPAPEVIETAINCC TSIIPNDDYFHVKDTDFNSVWHDIYRDIRASDSNSTKIYFNNIEIPLKLIADLINELGIN EFIDSKKELQMLSYNQVNKIINSNFPQQDLCFQTEKLLFTSLFQDPAFISALTSAFWQSL HITSSSVEHIYAQIMSENIENRLNFMPEQRVINNCGHIIKINAVVPKNDTAISASGGRAY EVSSSILPSHITCNGVGINKIETSYLVHAGTLPSSEGLRNAIPPESRQVSFAIISPDV
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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