Crystal Structure of Hec1 CH domain. Determined by X-ray diffraction at 1.8 Å resolution. Released 2 Jan 2007.
Explore 2IGP in 3D Show helices and sheets RCSB PDB PDBe
2IGP contains 5 α-helices and 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 89-105 | 17 | |
| α-helix | 122-133 | 12 | |
| β-strand | 144 | 1 | 1 |
| β-strand | 146 | 1 | 1 |
| α-helix | 147-157 | 11 | |
| α-helix | 166-170 | 5 | |
| α-helix | 178-194 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Retinoblastoma-associated protein HEC | A | protein | 120 | Homo sapiens | O14777 (AlphaFold model) |
>2IGP_1 Retinoblastoma-associated protein HEC (chains A) GSHMKDPRPLNDKAFIQQCIRQLCEFLTENGYAHNVSMKSLQAPSVKDFLKIFTFLYGFL CPSYELPDTKFEEEVPRIFKDLGYPFALSKSSMYTVGAPHTWPHIVAALVWLIDCIKIHT
The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment. Wei, R.R., Al-Bassam, J., Harrison, S.C. Nat Struct Mol Biol (2007) 14:54-59. DOI 10.1038/nsmb1186 · PubMed
Other PDB entries of the same protein (UniProt O14777 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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