Crystal Structure of the Human TAF4-TAF12 (TAFII135-TAFII20) Complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 26 Sept 2002.
Explore 1H3O in 3D Show helices and sheets RCSB PDB PDBe
1H3O contains 13 α-helices and 4 β-strands across 4 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 |
|---|---|---|---|
| α-helix | 873-885 | 13 | |
| β-strand | 891-892 | 2 | 1 |
| α-helix | 896-916 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 60-70 | 11 | |
| α-helix | 75-77 | 3 | |
| α-helix | 78-105 | 28 | |
| β-strand | 110-111 | 2 | 1 |
| α-helix | 113-119 | 7 | |
| α-helix | 120-124 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 873-887 | 15 | |
| β-strand | 891-892 | 2 | 2 |
| α-helix | 895-916 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 60-68 | 9 | |
| α-helix | 78-105 | 28 | |
| β-strand | 110-111 | 2 | 2 |
| α-helix | 113-119 | 7 | |
| α-helix | 120-124 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription initiation factor tfiid 135 kda subunit | A, C | protein | 75 | HOMO SAPIENS | O00268 (AlphaFold model) |
| Transcription initiation factor tfiid 20/15 kda subunits | B, D | protein | 76 | HOMO SAPIENS | Q16514 (AlphaFold model) |
>1H3O_1 TRANSCRIPTION INITIATION FACTOR TFIID 135 KDA SUBUNIT (chains A, C) MFLLQAPLQRRILEIGKKHGITELHPDVVSYVSHATQQRLQNLVEKISETAQQKNFSYKD DDRYEQASDVRAQLK
>1H3O_2 TRANSCRIPTION INITIATION FACTOR TFIID 20/15 KDA SUBUNITS (chains B, D) GSHMVLTKKKLQDLVREVDPNEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLE VKDVQLHLERQWNMWI
Crystal Structure of a Subcomplex of Human Transcription Factor TFIID Formed by TATA Binding Protein-Associated Factors Htaf4 (Htaf(II)135) and Htaf12 (Htaf(II)20). Werten, S., Mitschler, A., Romier, C. et al. J Biol Chem (2002) 277:45502. DOI 10.1074/JBC.M206587200 · PubMed
Other PDB entries of the same protein (UniProt O00268 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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