3WUT: Structure basis of inactivating cell abscission
Structure basis of inactivating cell abscission. Determined by X-ray diffraction at 2.3 Å resolution. Released 15 Jul 2015.
- Method
- X-ray diffraction
- Resolution
- 2.3 Å
- Organism
- Homo sapiens
- Chains
- 12
- Atoms
- 3,906
- Mol. weight
- 63.94 kDa
- Released
- 15 Jul 2015
Explore 3WUT in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3WUT contains 8 α-helices and 0 β-strands across 8 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.
Chain A: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 161-210 | 50 | |
Chain B: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 169-208 | 40 | |
Chain D: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 157-206 | 50 | |
Chains E and H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 160-206 | 47 | |
Chain G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 158-207 | 50 | |
Chain J: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 170-208 | 39 | |
Chain K: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 170-206 | 37 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Centrosomal protein of 55 kDa | A, B, D, E, G, H, J, K | protein | 63 | Homo sapiens | Q53EZ4 (AlphaFold model) |
| Inactive serine/threonine-protein kinase TEX14 | C, F, I, L | protein | 14 | Homo sapiens | Q8IWB6 (AlphaFold model) |
Sequence of entity 1 (A, B, D, E, G, H, J, K), FASTA
>3WUT_1 Centrosomal protein of 55 kDa (chains A, B, D, E, G, H, J, K)
GAMGSFNSSINNIHEMEIQLKDALEKNQQWLVYDQQREVYVKGLLAKIFELEKKTETAAH
SLP
Sequence of entity 2 (C, F, I, L), FASTA
>3WUT_2 Inactive serine/threonine-protein kinase TEX14 (chains C, F, I, L)
DLAVGPPSLNYIPP
Primary citation
Structural and biochemical insights into the role of testis-expressed gene 14 (TEX14) in forming the stable intercellular bridges of germ cells. Kim, H.J., Yoon, J., Matsuura, A. et al. Proc Natl Acad Sci U S A (2015) 112:12372-12377. DOI 10.1073/pnas.1418606112 · PubMed
Other PDB entries of the same protein (UniProt Q53EZ4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3E1R 2.0 Å, Midbody targeting of the ESCRT machinery by a non-canonical coiled-coil in CEP55
- 3WUV 2.79 Å, Structure basis of inactivating cell abscission with chimera peptide 2
- 3WUU 2.9 Å, Structure basis of inactivating cell abscission with chimera peptide 1
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