crystal structure of Arabidopsis ORC1b BAH-PHD cassette in complex with unmodified H3 peptide. Determined by X-ray diffraction at 1.9 Å resolution. Released 9 Mar 2016.
Explore 5HH7 in 3D Show helices and sheets RCSB PDB PDBe
5HH7 contains 12 α-helices and 17 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 |
|---|---|---|---|
| β-strand | 129-132 | 4 | 1 |
| β-strand | 134-137 | 4 | 2 |
| β-strand | 140-143 | 4 | 2 |
| β-strand | 147-150 | 4 | 1 |
| α-helix | 167-168 | 2 | |
| β-strand | 169 | 1 | 3 |
| β-strand | 180-182 | 3 | 3 |
| β-strand | 189-191 | 3 | 3 |
| α-helix | 192-194 | 3 | |
| α-helix | 198-199 | 2 | |
| α-helix | 202-204 | 3 | |
| α-helix | 210-214 | 5 | |
| α-helix | 238-243 | 6 | |
| β-strand | 248-258 | 11 | 1 |
| β-strand | 264-272 | 9 | 1 |
| α-helix | 274-276 | 3 | |
| β-strand | 289 | 1 | 4 |
| β-strand | 291-300 | 10 | 1 |
| α-helix | 301-303 | 3 | |
| β-strand | 304-308 | 5 | 1 |
| β-strand | 309-311 | 3 | 4 |
| α-helix | 313-316 | 4 | |
| α-helix | 317-319 | 3 | |
| β-strand | 326-328 | 3 | 4 |
| β-strand | 331-334 | 4 | 1 |
| β-strand | 339-342 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2 | 1 | |
| β-strand | 3 | 1 | 3 |
| α-helix | 4-5 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Origin of replication complex subunit 1B | A | protein | 233 | Arabidopsis thaliana | Q9SU24 (AlphaFold model) |
| Histone H3 1-15 peptide | P | protein | 15 | Arabidopsis thaliana | P59226 (AlphaFold model) |
>5HH7_1 Origin of replication complex subunit 1B (chains A) SSETIKKTKKKKRVYYNKVEFDETEFEIGDDVYVKRREDSNSDEEEDPEIEDCQICFKSD TNIMIECDDCLGGFHLKCLKPPLKEVPEGDWICQFCEVKKSGQSQTLDLPKPPEGKKLAR TMREKLLSGDLWAARIDKLWKEVDDGVYWIRARWYMIPEETVSGRQPHNLKRELYLTNDF ADIEMECILRHCSVKCPKEFSKASNDGDDVFLCEYEYDVHWRSFKRLAELADG
>5HH7_2 Histone H3 1-15 peptide (chains P) ARTKQTARKSTGGKA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Structural Basis for the Unique Multivalent Readout of Unmodified H3 Tail by Arabidopsis ORC1b BAH-PHD Cassette. Li, S., Yang, Z., Du, X. et al. Structure (2016) 24:486-494. DOI 10.1016/j.str.2016.01.004 · PubMed
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