CID of human RPRD1B. Determined by X-ray diffraction at 2.0 Å resolution. Released 17 Oct 2012.
Explore 4HFG in 3D Show helices and sheets RCSB PDB PDBe
4HFG contains 24 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-14 | 9 | |
| α-helix | 17-18 | 2 | |
| α-helix | 19-21 | 3 | |
| α-helix | 23-32 | 10 | |
| α-helix | 34-36 | 3 | |
| α-helix | 37-50 | 14 | |
| α-helix | 53-70 | 18 | |
| α-helix | 76-81 | 6 | |
| α-helix | 85-95 | 11 | |
| α-helix | 97 | 1 | |
| α-helix | 101-113 | 13 | |
| α-helix | 119-130 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-14 | 9 | |
| α-helix | 16-18 | 3 | |
| α-helix | 19-21 | 3 | |
| α-helix | 23-32 | 10 | |
| α-helix | 34-36 | 3 | |
| α-helix | 37-50 | 14 | |
| α-helix | 56-70 | 15 | |
| α-helix | 76-82 | 7 | |
| α-helix | 85-95 | 11 | |
| α-helix | 97 | 1 | |
| α-helix | 101-113 | 13 | |
| α-helix | 119-129 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulation of nuclear pre-mRNA domain-containing protein 1B | A, B | protein | 135 | Homo sapiens | Q9NQG5 (AlphaFold model) |
>4HFG_1 Regulation of nuclear pre-mRNA domain-containing protein 1B (chains A, B) GSSFSESALEKKLSELSNSQHSVQTLSLWLIHHRKHAGPIVSVWHRELRKAKSNRKLTFL YLANDVIQNSKRKGPEFTREFESVLVDAFSHVAREADEGCKKPLERLLNIWQERSVYGGE FIQQLKLSMEDSKSP
CID of human RPRD1B. Ni, Z., Xu, C., Tempel, W. et al. To be published.
Other PDB entries of the same protein (UniProt Q9NQG5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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