Crystal structure of human Ig-beta homodimer. Determined by X-ray diffraction at 3.2 Å resolution. Released 25 Aug 2010.
Explore 3KG5 in 3D Show helices and sheets RCSB PDB PDBe
3KG5 contains 2 α-helices and 22 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 |
|---|---|---|---|
| β-strand | 47-49 | 3 | 1 |
| β-strand | 52-56 | 5 | 2 |
| β-strand | 61-66 | 6 | 1 |
| β-strand | 75-79 | 5 | 2 |
| β-strand | 87-88 | 2 | 2 |
| α-helix | 89-91 | 3 | |
| β-strand | 96-100 | 5 | 1 |
| β-strand | 104-109 | 6 | 1 |
| β-strand | 118-125 | 8 | 2 |
| β-strand | 132-134 | 3 | 2 |
| β-strand | 138-143 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 47-49 | 3 | 3 |
| β-strand | 52-56 | 5 | 4 |
| β-strand | 60-63 | 4 | 5 |
| β-strand | 64-66 | 3 | 3 |
| β-strand | 74-79 | 6 | 4 |
| β-strand | 87-88 | 2 | 4 |
| β-strand | 96-98 | 3 | 5 |
| β-strand | 104 | 1 | 3 |
| β-strand | 107-110 | 4 | 5 |
| α-helix | 114-116 | 3 | |
| β-strand | 118-125 | 8 | 4 |
| β-strand | 132-134 | 3 | 4 |
| β-strand | 138-143 | 6 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| B-cell antigen receptor complex-associated protein beta chain | A, B | protein | 134 | Homo sapiens | P40259 (AlphaFold model) |
>3KG5_1 B-cell antigen receptor complex-associated protein beta chain (chains A, B) VPAARSEDRYRNPKGSACSRIWQSPRFIARKRGFTVKMHCYMNSASGNVSWLWKQEMDEN PQQLKLEKGRMEESQNESLATLTIQGIRFEDNGIYFCQQKCNNTSEVYQGCGTELRVMGF STLAQLKQRNTLKD
Structural and Functional Studies of Igalphabeta and Its Assembly with the B Cell Antigen Receptor. Radaev, S., Zou, Z., Tolar, P. et al. Structure (2010) 18:934-943. DOI 10.1016/j.str.2010.04.019 · PubMed
Other PDB entries of the same protein (UniProt P40259 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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