3VTW: T7-tagged Optineurin LIR-fused human LC3B_2-119

Crystal structure of T7-tagged Optineurin LIR-fused human LC3B_2-119. Determined by X-ray diffraction at 2.52 Å resolution. Released 26 Jun 2013.

Method
X-ray diffraction
Resolution
2.52 Å
Organism
Homo sapiens
Chains
3
Atoms
3,207
Mol. weight
51.91 kDa
Released
26 Jun 2013

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

Secondary structure: helices and β-sheets

3VTW contains 21 α-helices and 21 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.

Chain A: 7 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix17-215
α-helix22-254
α-helix28-4114
β-strand45-5281
α-helix60-623
β-strand66-7051
β-strand7412
α-helix75-8511
β-strand95-9841
β-strand101-10221
β-strand10912
α-helix110-1178
α-helix1231
β-strand124-12961
Chain B: 7 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix18-214
α-helix22-254
α-helix28-4114
β-strand45-5283
α-helix60-623
β-strand66-7053
β-strand7414
α-helix75-8612
β-strand95-9843
β-strand101-10223
β-strand10914
α-helix110-1178
α-helix1231
β-strand124-12963
Chain C: 7 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix18-214
α-helix22-254
α-helix28-4114
β-strand45-5285
α-helix60-623
β-strand66-7055
β-strand7416
α-helix75-8511
β-strand95-9845
β-strand10115
β-strand10916
α-helix110-1178
α-helix1231
β-strand124-12965

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Optineurin, microtubule-associated proteins 1A/1B light chain 3BA, B, Cprotein149Homo sapiensQ96CV9 (AlphaFold model), Q9GZQ8 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>3VTW_1 Optineurin, microtubule-associated proteins 1A/1B light chain 3B (chains A, B, C)
GSHMASMTGGQQMGRGSEEGEEEDEFVEIGGPSEKTFKQRRTFEQRVEDVRLIREQHPTK
IPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVS
VSTPISEVYESEKDEDGFLYMVYASQETF

Primary citation

Structural basis for phosphorylation-triggered autophagic clearance of Salmonella. Rogov, V.V., Suzuki, H., Fiskin, E. et al. Biochem J (2013) 454:459-466. DOI 10.1042/BJ20121907 · PubMed

Other PDB entries of the same protein (UniProt Q96CV9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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