Crystal structure of the TCERG1 FF4-6 tandem repeat domain. Determined by X-ray diffraction at 2.0 Å resolution. Released 27 Feb 2013.
Explore 4FQG in 3D Show helices and sheets RCSB PDB PDBe
4FQG contains 22 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 2-19 | 18 | |
| α-helix | 27-34 | 8 | |
| α-helix | 38-43 | 6 | |
| α-helix | 48-75 | 28 | |
| α-helix | 86-93 | 8 | |
| α-helix | 97-100 | 4 | |
| α-helix | 106-134 | 29 | |
| α-helix | 142-148 | 7 | |
| α-helix | 151-160 | 10 | |
| α-helix | 164-167 | 4 | |
| α-helix | 173-185 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-19 | 17 | |
| α-helix | 27-34 | 8 | |
| α-helix | 38-43 | 6 | |
| α-helix | 48-75 | 28 | |
| α-helix | 86-93 | 8 | |
| α-helix | 97-100 | 4 | |
| α-helix | 106-134 | 29 | |
| α-helix | 142-148 | 7 | |
| α-helix | 151-160 | 10 | |
| α-helix | 164-167 | 4 | |
| α-helix | 173-187 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription elongation regulator 1 | A, B | protein | 190 | Homo sapiens | O14776 (AlphaFold model) |
>4FQG_1 Transcription elongation regulator 1 (chains A, B) SHMKREEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIE ALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRDK YITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRKLI VAYVDDLDRR
| ID | Name | Formula | Copies |
|---|---|---|---|
| NI | Nickel (II) ion | Ni | 2 |
Water and common crystallization additives (CL) are not listed.
Specific Interaction of the Transcription Elongation Regulator TCERG1 with RNA Polymerase II Requires Simultaneous Phosphorylation at Ser2, Ser5, and Ser7 within the Carboxyl-terminal Domain Repeat. Liu, J., Fan, S., Lee, C.J. et al. J Biol Chem (2013) 288:10890-10901. DOI 10.1074/jbc.M113.460238 · PubMed
Other PDB entries of the same protein (UniProt O14776 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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