9B9Q: Type 1 encapsulin shell protein EncA

Cargo-loaded Myxococcus xanthus EncA encapsulin engineered pore mutant with T=3 icosahedral symmetry. Determined by electron microscopy at 3.14 Å resolution. Released 18 Sept 2024.

Method
Electron microscopy
Resolution
3.14 Å
Organism
Myxococcus xanthus DK 1622
Chains
6
Atoms
6,569
Mol. weight
96.95 kDa
Released
18 Sept 2024

Explore 9B9Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9B9Q contains 33 α-helices and 34 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: 12 helices, 10 β-strands

ElementResiduesLengthSheet
α-helix14-3118
α-helix391
β-strand4011
α-helix41-433
β-strand50-5122
α-helix75-773
β-strand83-8422
α-helix85-862
β-strand88-9471
α-helix96-1038
α-helix107-1104
α-helix112-13019
α-helix160-17415
β-strand181-18553
α-helix187-1926
α-helix198-2069
β-strand207-21263
β-strand221-22553
β-strand232-243121
β-strand251-262121
α-helix266-2683
β-strand269-27133
Chain B: 10 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix14-3118
α-helix34-363
β-strand40-4344
β-strand50-5125
α-helix72-754
β-strand83-8425
α-helix851
β-strand88-9474
α-helix96-10510
α-helix112-13019
α-helix162-17514
β-strand181-18556
α-helix187-1959
α-helix198-2069
β-strand210-21236
β-strand221-22556
β-strand231-243134
β-strand24717
β-strand25017
β-strand251-263134
α-helix266-2683
β-strand269-27136
Chain C: 11 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix14-3118
α-helix34-363
β-strand42-4328
β-strand50-5349
α-helix73-753
β-strand81-8449
α-helix85-862
β-strand88-9478
α-helix96-10510
α-helix107-1104
α-helix112-13019
α-helix160-17314
β-strand181-185510
α-helix187-1926
α-helix198-2058
β-strand209-212410
β-strand221-225510
β-strand231-243138
β-strand247111
β-strand250111
β-strand251-263138
α-helix266-2683
β-strand269-271310

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Type 1 encapsulin shell protein EncAA, B, Cprotein281Myxococcus xanthus DK 1622Q1D6H4 (AlphaFold model)
Encapsulin nanocompartment cargo protein EncCF, G, Hprotein12Myxococcus xanthus DK 1622Q1D3Y8 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>9B9Q_1 Type 1 encapsulin shell protein EncA (chains A, B, C)
MPDFLGHAENPLREEEWARLNETVIQVARRSLVGRRILDIYGPLGAGVQTVPYDEFQGVS
PGAVDIVGEQETAMVFTDARKFKTIPIIYKDFLLHWRDIEAARTHNMPLDVSAAAGAAAL
CAQQEDELIFYGDARLGYEGLMTANGRLTVPLGDWTSPGGGFQAIVEATRKLNEQGHFGP
YAVVLSPRLYSQLHRGGEIETIRQLASDGVYQSNRLRGESGVVVSTGRENMDLAVSMDMV
AAYLGASRMNHPFRVLEALLLRIKHPDAICTLEGAGATERR
Sequence of entity 2 (F, G, H), FASTA
>9B9Q_2 Encapsulin nanocompartment cargo protein EncC (chains F, G, H)
PEKRLTVGSLRR

Primary citation

Pore Engineering as a General Strategy to Improve Protein-Based Enzyme Nanoreactor Performance. Kwon, S., Andreas, M.P., Giessen, T.W. ACS Nano (2024) 18:25740-25753. DOI 10.1021/acsnano.4c08186 · PubMed

Other PDB entries of the same protein (UniProt Q1D6H4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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