3HYM: Anaphase-promoting complex subunit CDC26
Insights into Anaphase Promoting Complex TPR subdomain assembly from a CDC26-APC6 structure. Determined by X-ray diffraction at 2.8 Å resolution. Released 11 Aug 2009.
- Method
- X-ray diffraction
- Resolution
- 2.8 Å
- Organism
- Homo sapiens
- Chains
- 12
- Atoms
- 15,517
- Mol. weight
- 249.12 kDa
- Released
- 11 Aug 2009
Explore 3HYM in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3HYM contains 117 α-helices and 0 β-strands across 12 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 I: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14-16 | 3 | |
| α-helix | 17-25 | 9 | |
Chain B: 18 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 234-243 | 10 | |
| α-helix | 247-260 | 14 | |
| α-helix | 268-278 | 11 | |
| α-helix | 281-294 | 14 | |
| α-helix | 300-311 | 12 | |
| α-helix | 316-327 | 12 | |
| α-helix | 335-347 | 13 | |
| α-helix | 350-363 | 14 | |
| α-helix | 369-380 | 12 | |
| α-helix | 384-395 | 12 | |
| α-helix | 402-414 | 13 | |
| α-helix | 418-430 | 13 | |
| α-helix | 431-435 | 5 | |
| α-helix | 446-457 | 12 | |
| α-helix | 461-474 | 14 | |
| α-helix | 480-492 | 13 | |
| α-helix | 495-503 | 9 | |
| α-helix | 513-524 | 12 | |
Chain C: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-21 | 5 | |
Chain D: 17 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 232-244 | 13 | |
| α-helix | 247-260 | 14 | |
| α-helix | 268-277 | 10 | |
| α-helix | 281-294 | 14 | |
| α-helix | 300-310 | 11 | |
| α-helix | 316-329 | 14 | |
| α-helix | 334-345 | 12 | |
| α-helix | 350-363 | 14 | |
| α-helix | 369-379 | 11 | |
| α-helix | 384-397 | 14 | |
| α-helix | 402-414 | 13 | |
| α-helix | 420-433 | 14 | |
| α-helix | 446-458 | 13 | |
| α-helix | 461-474 | 14 | |
| α-helix | 479-492 | 14 | |
| α-helix | 495-506 | 12 | |
| α-helix | 513-524 | 12 | |
Chain E: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-7 | 3 | |
| α-helix | 13-16 | 4 | |
| α-helix | 17-25 | 9 | |
Chain F: 17 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 232-243 | 12 | |
| α-helix | 247-260 | 14 | |
| α-helix | 268-277 | 10 | |
| α-helix | 283-294 | 12 | |
| α-helix | 300-306 | 7 | |
| α-helix | 316-327 | 12 | |
| α-helix | 334-347 | 14 | |
| α-helix | 350-363 | 14 | |
| α-helix | 369-379 | 11 | |
| α-helix | 384-395 | 12 | |
| α-helix | 402-413 | 12 | |
| α-helix | 418-433 | 16 | |
| α-helix | 446-457 | 12 | |
| α-helix | 461-474 | 14 | |
| α-helix | 479-492 | 14 | |
| α-helix | 495-506 | 12 | |
| α-helix | 513-524 | 12 | |
Chain G: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-7 | 4 | |
| α-helix | 17-24 | 8 | |
Chain H: 18 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 234-243 | 10 | |
| α-helix | 247-260 | 14 | |
| α-helix | 268-277 | 10 | |
| α-helix | 281-294 | 14 | |
| α-helix | 300-311 | 12 | |
| α-helix | 316-327 | 12 | |
| α-helix | 334-346 | 13 | |
| α-helix | 350-363 | 14 | |
| α-helix | 369-379 | 11 | |
| α-helix | 384-395 | 12 | |
| α-helix | 402-414 | 13 | |
| α-helix | 418-427 | 10 | |
| α-helix | 441-443 | 3 | |
| α-helix | 446-457 | 12 | |
| α-helix | 461-474 | 14 | |
| α-helix | 479-492 | 14 | |
| α-helix | 495-506 | 12 | |
| α-helix | 513-526 | 14 | |
3 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Anaphase-promoting complex subunit CDC26 | A, C, E, G, I, K | protein | 29 | Homo sapiens | Q8NHZ8 (AlphaFold model) |
| Cell division cycle protein 16 homolog | B, D, F, H, J, L | protein | 330 | Homo sapiens | Q13042 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G, I, K), FASTA
>3HYM_1 Anaphase-promoting complex subunit CDC26 (chains A, C, E, G, I, K)
MLRRKPTRLELKLDDIEEFENIRKDLETR
Sequence of entity 2 (B, D, F, H, J, L), FASTA
>3HYM_2 Cell division cycle protein 16 homolog (chains B, D, F, H, J, L)
GSYNKPSETVIPESVDGLQENLDVVVSLAERHYYNCDFKMCYKLTSVVMEKDPFHASCLP
VHIGTLVELNKANELFYLSHKLVDLYPSNPVSWFAVGCYYLMVGHKNEHARRYLSKATTL
EKTYGPAWIAYGHSFAVESEHDQAMAAYFTAAQLMKGCHLPMLYIGLEYGLTNNSKLAER
FFSQALSIAPEDPFVMHEVGVVAFQNGEWKTAEKWFLDALEKIKAIGNEVTVDKWEPLLN
NLGHVCRKLKKYAEALDYHRQALVLIPQNASTYSAIGYIHSLMGNFENAVDYFHTALGLR
RDDTFSVTMLGHCIEMYIGDSEAYIGADIK
Primary citation
Insights into anaphase promoting complex TPR subdomain assembly from a CDC26-APC6 structure. Wang, J., Dye, B.T., Rajashankar, K.R. et al. Nat Struct Mol Biol (2009) 16:987-989. DOI 10.1038/nsmb.1645 · PubMed
Other PDB entries of the same protein (UniProt Q8NHZ8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9GAW 2.9 Å, High-resolution structure of the Anaphase-promoting complex/cyclosome (APC/C) bound to…
- 6Q6G 3.2 Å, Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D1 box class
- 6Q6H 3.2 Å, Cryo-EM structure of the APC/C-Cdc20-Cdk2-cyclinA2-Cks2 complex, the D2 box class
- 8PKP 3.2 Å, Cryo-EM structure of the apo Anaphase-promoting complex/cyclosome (APC/C) at 3.2…
- 5G05 3.4 Å, Cryo-EM structure of combined apo phosphorylated APC
- 8TAU 3.5 Å, APC/C-CDH1-UBE2C-UBE2S-Ubiquitin-CyclinB
- 4UI9 3.6 Å, Atomic structure of the human Anaphase-Promoting Complex
- 6TNT 3.78 Å, SUMOylated apoAPC/C with repositioned APC2 WHB domain
- 6TLJ 3.8 Å, Cryo-EM structure of the Anaphase-promoting complex/Cyclosome, in complex with the…
- 5G04 3.9 Å, Structure of the human APC-Cdc20-Hsl1 complex
- 6TM5 3.9 Å, Cryo-EM structure of the Anaphase-promoting complex/Cyclosome, in complex with the Nek2A…
- 9N9R 3.9 Å, Model of APC/C-CDC20-UBE2C from H2A/H2B-bound complex
Browse structure collections
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