Solution structure of the phd domain from the kap-1 corepressor. Determined by solution NMR. Released 24 Jan 2001.
Explore 1FP0 in 3D Show helices and sheets RCSB PDB PDBe
1FP0 contains 0 α-helices and 4 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 |
|---|---|---|---|
| β-strand | 38-39 | 2 | 1 |
| β-strand | 46-47 | 2 | 1 |
| β-strand | 61 | 1 | 2 |
| β-strand | 63 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kap-1 corepressor | A | protein | 88 | Homo sapiens | Q13263 (AlphaFold model) |
>1FP0_1 KAP-1 COREPRESSOR (chains A) MRGSHHHHHHGSDIIDEFGTLDDSATICRVCQKPGDLVMCNQCEFCFHLDCHLPALQDVP GEEWSCSLCHVLPDLKEEDVDLQACKLN
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains. Capili, A.D., Schultz, D.C., RauscherIII, F.J. et al. EMBO J (2001) 20:165-177. DOI 10.1093/emboj/20.1.165 · PubMed
Other PDB entries of the same protein (UniProt Q13263 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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