4D6K: DNTTIP1 dimerisation domain
Structure of DNTTIP1 dimerisation domain. Determined by X-ray diffraction at 2.1 Å resolution. Released 18 Feb 2015.
- Method
- X-ray diffraction
- Resolution
- 2.1 Å
- Organism
- HOMO SAPIENS
- Chains
- 6
- Atoms
- 3,504
- Mol. weight
- 62.55 kDa
- Released
- 18 Feb 2015
Explore 4D6K in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4D6K contains 24 α-helices and 0 β-strands across 6 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: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 65-87 | 23 | |
| α-helix | 90-103 | 14 | |
| α-helix | 110-125 | 16 | |
| α-helix | 126-129 | 4 | |
Chain B: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 63-87 | 25 | |
| α-helix | 90-104 | 15 | |
| α-helix | 110-125 | 16 | |
| α-helix | 126-129 | 4 | |
Chain C: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 66-87 | 22 | |
| α-helix | 90-104 | 15 | |
| α-helix | 110-125 | 16 | |
| α-helix | 126-129 | 4 | |
Chain D: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 64-87 | 24 | |
| α-helix | 90-103 | 14 | |
| α-helix | 110-125 | 16 | |
| α-helix | 126-129 | 4 | |
Chain E: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 63-87 | 25 | |
| α-helix | 90-103 | 14 | |
| α-helix | 110-125 | 16 | |
| α-helix | 126-129 | 4 | |
Chain F: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 67-87 | 21 | |
| α-helix | 90-102 | 13 | |
| α-helix | 110-125 | 16 | |
| α-helix | 126-129 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Deoxynucleotidyltransferase terminal-interacting protein 1 | A, B, C, D, E, F | protein | 92 | HOMO SAPIENS | Q9H147 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>4D6K_1 DEOXYNUCLEOTIDYLTRANSFERASE TERMINAL-INTERACTING PROTEIN 1 (chains A, B, C, D, E, F)
MTTSFTDPAISMDLLRAVLQPSINEEIQTVFNKYMKFFQKAALNVRDNVGEEVDAEQLIQ
EACRSCLEQAKLLFSDGEKVIPRLTHELPGIK
Primary citation
Structural and Functional Characterization of a Cell Cycle Associated Hdac1/2 Complex Reveals the Structural Basis for Complex Assembly and Nucleosome Targeting. Itoh, T., Fairall, L., Muskett, F.W. et al. Nucleic Acids Res (2015) 43:2033. DOI 10.1093/NAR/GKV068 · PubMed
Other PDB entries of the same protein (UniProt Q9H147 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9R4I 2.92 Å, An auto inhibitory loop in the MiDAC histone deacetylase complex
- 6Z2J 4.0 Å, The structure of the dimeric HDAC1/MIDEAS/DNTTIP1 MiDAC deacetylase complex
- 6Z2K 4.5 Å, The structure of the tetrameric HDAC1/MIDEAS/DNTTIP1 MiDAC deacetylase complex
- 2MWI The structure of the carboxy-terminal domain of DNTTIP1
Browse structure collections
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