6J7W: Human BCMA

Crystal Structure of Human BCMA in complex with UniAb(TM) VH. Determined by X-ray diffraction at 2.6 Å resolution. Released 6 Feb 2019.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Homo sapiens
Chains
4
Atoms
2,345
Mol. weight
33.89 kDa
Released
6 Feb 2019

Explore 6J7W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6J7W contains 7 α-helices and 26 β-strands across 4 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 and B: 2 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand3-751
β-strand10-1232
β-strand18-2581
α-helix29-313
β-strand34-3962
β-strand46-5162
β-strand58-6032
β-strand68-7361
β-strand78-8361
α-helix88-903
β-strand92-9982
β-strand106-10942
β-strand113-11752
Chain C: 1 helix, 2 β-strands
ElementResiduesLengthSheet
β-strand11-1443
β-strand19-2243
α-helix24-274
Chain D: 2 helices, 2 β-strands
ElementResiduesLengthSheet
β-strand11-1446
β-strand19-2246
α-helix23-253
α-helix34-363

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
UniAbA, Bprotein118Homo sapiens
Tumor necrosis factor receptor superfamily member 17C, Dprotein39Homo sapiensQ02223 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6J7W_1 UniAb (chains A, B)
EVQLVESGGGLVQPGGSLRLSCAASGFTVSSYGMSWVRQAPGKGPEWVSGIRGSDGSTYY
ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKQGENDGPFDHRGQGTLVTVS
Sequence of entity 2 (C, D), FASTA
>6J7W_2 Tumor necrosis factor receptor superfamily member 17 (chains C, D)
GQCSQNEYFDSLLHACIPCQLRCSSNTPPLTCQRYCNAS

Primary citation

Multispecific Antibody Development Platform Based on Human Heavy Chain Antibodies. Clarke, S.C., Ma, B., Trinklein, N.D. et al. Front Immunol (2018) 9:3037-3037. DOI 10.3389/fimmu.2018.03037 · PubMed

Other PDB entries of the same protein (UniProt Q02223 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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