1YIG: Human EB1 C-terminal Dimerization Domain

Crystal Structure of the Human EB1 C-terminal Dimerization Domain. Determined by X-ray diffraction at 2.0 Å resolution. Released 8 Mar 2005.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
2
Atoms
1,071
Mol. weight
17.23 kDa
Released
8 Mar 2005

Explore 1YIG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1YIG contains 7 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: 4 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix191-23040
α-helix232-2343
α-helix237-24711
α-helix251-2533
Chain B: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix191-23040
α-helix232-2343
α-helix237-24610

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Microtubule-associated protein RP/EB family member 1A, Bprotein76Homo sapiensQ15691 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1YIG_1 Microtubule-associated protein RP/EB family member 1 (chains A, B)
GPLGSGVGNGDDEAAELMQQVNVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVL
QRIMDILYATDEGFVI

Primary citation

Structural determinants for EB1-mediated recruitment of APC and spectraplakins to the microtubule plus end. Slep, K.C., Rogers, S.L., Elliott, S.L. et al. J Cell Biol (2005) 168:587-598. DOI 10.1083/jcb.200410114 · PubMed

Other PDB entries of the same protein (UniProt Q15691 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 1YIG 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.