2KIS: CA150 FF1 domain and FF1-FF2 interdomain linker

Solution structure of CA150 FF1 domain and FF1-FF2 interdomain linker. Determined by solution NMR. Released 8 Sept 2009.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
602
Mol. weight
8.58 kDa
Released
8 Sept 2009

Explore 2KIS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2KIS contains 4 α-helices and 0 β-strands across 1 chain. 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

ElementResiduesLengthSheet
α-helix618-63215
α-helix642-6487
α-helix651-6544
α-helix660-68021

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcription elongation regulator 1Aprotein71Homo sapiensO14776 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2KIS_1 Transcription elongation regulator 1 (chains A)
GAMGSLEARMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYLLLNPKERKQVFDQYVKTR
AEEERREKKNK

Primary citation

Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays. Murphy, J.M., Hansen, D.F., Wiesner, S. et al. J Mol Biol (2009) 393:409-424. DOI 10.1016/j.jmb.2009.08.049 · 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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