Mouse IgG2a in complex with mouse TRIM21 PRYSPRY. Determined by X-ray diffraction at 1.99 Å resolution. Released 22 May 2013.
Explore 3ZO0 in 3D Show helices and sheets RCSB PDB PDBe
3ZO0 contains 14 α-helices and 36 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 | 239-243 | 5 | 1 |
| α-helix | 244-246 | 3 | |
| α-helix | 247-251 | 5 | |
| β-strand | 258-266 | 9 | 1 |
| β-strand | 274-279 | 6 | 2 |
| β-strand | 282-284 | 3 | 2 |
| β-strand | 288-295 | 8 | 1 |
| β-strand | 299-307 | 9 | 1 |
| α-helix | 310-314 | 5 | |
| β-strand | 319-324 | 6 | 2 |
| β-strand | 332-336 | 5 | 2 |
| α-helix | 338-340 | 3 | |
| β-strand | 344 | 1 | 3 |
| α-helix | 345-346 | 2 | |
| β-strand | 347-351 | 5 | 4 |
| α-helix | 352-354 | 3 | |
| α-helix | 355-358 | 4 | |
| β-strand | 362-372 | 11 | 4 |
| β-strand | 373 | 1 | 3 |
| β-strand | 378-383 | 6 | 5 |
| β-strand | 386-387 | 2 | 5 |
| α-helix | 388 | 1 | |
| β-strand | 391-393 | 3 | 4 |
| α-helix | 394-396 | 3 | |
| β-strand | 397-398 | 2 | 4 |
| β-strand | 404-413 | 10 | 4 |
| α-helix | 414-418 | 5 | |
| β-strand | 423-428 | 6 | 5 |
| α-helix | 433-435 | 3 | |
| β-strand | 436-441 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8 | 1 | 6 |
| β-strand | 13 | 1 | 7 |
| α-helix | 15-17 | 3 | |
| β-strand | 22-24 | 3 | 6 |
| β-strand | 30-33 | 4 | 6 |
| β-strand | 52-54 | 3 | 8 |
| β-strand | 55 | 1 | 7 |
| β-strand | 59 | 1 | 8 |
| β-strand | 63-69 | 7 | 6 |
| β-strand | 76-82 | 7 | 8 |
| α-helix | 95-97 | 3 | |
| β-strand | 99-105 | 7 | 8 |
| β-strand | 108-111 | 4 | 8 |
| β-strand | 117-118 | 2 | 8 |
| β-strand | 127-133 | 7 | 6 |
| β-strand | 138-143 | 6 | 6 |
| β-strand | 149-154 | 6 | 6 |
| β-strand | 163-168 | 6 | 8 |
| α-helix | 179-180 | 2 | |
| β-strand | 181-183 | 3 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ig gamma-2A chain C region, A allele | A | protein | 208 | MUS MUSCULUS | P01868 (AlphaFold model) |
| E3 ubiquitin-protein ligase TRIM21 | B | protein | 182 | MUS MUSCULUS | Q62191 (AlphaFold model) |
>3ZO0_1 IG GAMMA-2A CHAIN C REGION, A ALLELE (chains A) GPSVFIFPPKIKDVLMISLSPIVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDY NSTLRVVSALPIQHQDWMSGKEFKCKVNNKDLPAPIERTISKPKGSVRAPQVYVLPPPEE EMTKKQVTLTCMVTDFMPEDIYVEWTNNGKTELNYKNTEPVLDSDGSYFMYSKLRVEKKN WVERNSYSCSVVHEGLHNHHTTKSFSRS
>3ZO0_2 E3 UBIQUITIN-PROTEIN LIGASE TRIM21 (chains B) HMVHITLDRNTANSWLIISKDRRQVRMGDTHQNVSDNKERFSNYPMVLGAQRFSSGKMYW EVDVTQKEAWDLGVCRDSVQRKGQFSLSPENGFWTIWLWQKSYEAGTSPQTTLHIQVPPC QIGIFVDYEAGVVSFYNITDHGSLIYTFSECVFAGPLRPFFNVGFNYSGGNAAPLKLCPL KM
Trim21 is an Igg Receptor that is Structurally, Thermodynamically, and Kinetically Conserved. Keeble, A.H., Khan, Z., Forster, A. et al. Proc Natl Acad Sci U S A (2008) 105:6045. DOI 10.1073/PNAS.0800159105 · PubMed
Other PDB entries of the same protein (UniProt P01868 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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