4FQG: TCERG1 FF4-6 tandem repeat domain

Crystal structure of the TCERG1 FF4-6 tandem repeat domain. Determined by X-ray diffraction at 2.0 Å resolution. Released 27 Feb 2013.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
2
Atoms
3,698
Mol. weight
46.33 kDa
Ligands
NI
Released
27 Feb 2013

Explore 4FQG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 11 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix2-1918
α-helix27-348
α-helix38-436
α-helix48-7528
α-helix86-938
α-helix97-1004
α-helix106-13429
α-helix142-1487
α-helix151-16010
α-helix164-1674
α-helix173-18513
Chain B: 11 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix3-1917
α-helix27-348
α-helix38-436
α-helix48-7528
α-helix86-938
α-helix97-1004
α-helix106-13429
α-helix142-1487
α-helix151-16010
α-helix164-1674
α-helix173-18715

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcription elongation regulator 1A, Bprotein190Homo sapiensO14776 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4FQG_1 Transcription elongation regulator 1 (chains A, B)
SHMKREEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIE
ALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRDK
YITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRKLI
VAYVDDLDRR

Ligands and cofactors

IDNameFormulaCopies
NINickel (II) ionNi2

Water and common crystallization additives (CL) are not listed.

Primary citation

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:

Browse structure collections

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