6R80: AFF4 C-terminal homology domain

Structure of AFF4 C-terminal homology domain. Determined by X-ray diffraction at 2.2 Å resolution. Released 12 Jun 2019.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
1
Atoms
1,853
Mol. weight
32.3 kDa
Released
12 Jun 2019

Explore 6R80 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6R80 contains 10 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: 10 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix915-93117
α-helix935-95925
α-helix967-98115
α-helix993-101624
α-helix1018-103922
α-helix1041-10422
α-helix1087-111731
α-helix1118-11203
α-helix1121-113111
α-helix1141-115919

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
AF4/FMR2 family member 4Aprotein284Homo sapiensQ9UHB7 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6R80_1 AF4/FMR2 family member 4 (chains A)
MGSSHHHHHHENLYFQSNASKPRRTKLVFDDRNYSADHYLQEAKKLKHNADALSDRFEKA
VYYLDAVVSFIECGNALEKNAQESKSPFPMYSETVDLIKYTMKLKNYLAPDATAADKRLT
VLCLRCESLLYLRLFKLKKENALKYSKTLTEHLKNSYNNSQAPSPGLGSKAVGMPSPVSP
KLSPGNSGNYSSGASSASASGSSVTIPQKIHQMAASYVQVTSNFLYATEIWDQAEQLSKE
QKEFFAELDKVMGPLIFNASIMTDLVRYTRQGLHWLRQDAKLIS

Primary citation

Structure of the super-elongation complex subunit AFF4 C-terminal homology domain reveals requirements for AFF homo- and heterodimerization. Chen, Y., Cramer, P. J Biol Chem (2019) 294:10663-10673. DOI 10.1074/jbc.RA119.008577 · PubMed

Other PDB entries of the same protein (UniProt Q9UHB7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 6R80 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.