Crystal structure of human CD22 Ig domains 1-3. Determined by X-ray diffraction at 2.12 Å resolution. Released 4 Oct 2017.
Explore 5VKJ in 3D Show helices and sheets RCSB PDB PDBe
5VKJ contains 6 α-helices and 31 β-strands across 1 chain. 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 | 21-23 | 3 | |
| β-strand | 24-27 | 4 | 1 |
| β-strand | 31-35 | 5 | 2 |
| β-strand | 40-42 | 3 | 3 |
| β-strand | 45-48 | 4 | 1 |
| β-strand | 55-65 | 11 | 2 |
| β-strand | 70-78 | 9 | 2 |
| α-helix | 82-84 | 3 | |
| β-strand | 92-94 | 3 | 3 |
| β-strand | 101 | 1 | 1 |
| β-strand | 104-106 | 3 | 3 |
| α-helix | 111-113 | 3 | |
| β-strand | 115-122 | 8 | 2 |
| β-strand | 127-137 | 11 | 2 |
| α-helix | 140-142 | 3 | |
| β-strand | 144-146 | 3 | 4 |
| β-strand | 152 | 1 | 5 |
| β-strand | 157-163 | 7 | 4 |
| β-strand | 172-178 | 7 | 6 |
| β-strand | 181-182 | 2 | 6 |
| β-strand | 187-193 | 7 | 4 |
| β-strand | 198-206 | 9 | 4 |
| α-helix | 210-212 | 3 | |
| β-strand | 216-223 | 8 | 6 |
| β-strand | 228-235 | 8 | 6 |
| β-strand | 239 | 1 | 5 |
| β-strand | 240-249 | 10 | 7 |
| β-strand | 254-255 | 2 | 8 |
| β-strand | 261-271 | 11 | 7 |
| β-strand | 276-281 | 6 | 9 |
| β-strand | 284-286 | 3 | 9 |
| β-strand | 293-296 | 4 | 7 |
| α-helix | 301-303 | 3 | |
| β-strand | 305-312 | 8 | 9 |
| β-strand | 317-319 | 3 | 9 |
| β-strand | 323-325 | 3 | 9 |
| β-strand | 326-327 | 2 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| B-cell receptor CD22 | A | protein | 324 | Homo sapiens | P20273 (AlphaFold model) |
>5VKJ_1 B-cell receptor CD22 (chains A) ETGDSSKWVFEHPETLYAWEGACVWIPCTYRALDGDLESFILFHNPEYNKATSKFDGTRL YESTKDGKVPSEQKRVQFLGDKNKNCTLSIHPVHLADSGQLGLRMESKTEKWMERIHLAV SERPFPPHIQLPPEIQESQEVTLTCLLAFSCYGYPIQLQWLLEGVPMRQAAVTSTSLTIK SVFTRSELKFSPQWSHHGKIVTCQLQDADGKFLSADTVQLNVKHTPKLEIKVTPSDAIVR EGDSVTMTCEVSSSNPEYTTVSWLKDGTSLKKQNTFTLNLREVTKDQSGKYCCQVSNDVG PGRSEEVFLQVQYAGGTKHHHHHH
Molecular basis of human CD22 function and therapeutic targeting. Ereno-Orbea, J., Sicard, T., Cui, H. et al. Nat Commun (2017) 8:764-764. DOI 10.1038/s41467-017-00836-6 · PubMed
Other PDB entries of the same protein (UniProt P20273 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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