Crystal Structure of Rev-Erb beta. Determined by X-ray diffraction at 2.4 Å resolution. Released 23 Oct 2007.
Explore 2V0V in 3D Show helices and sheets RCSB PDB PDBe
2V0V contains 46 α-helices and 10 β-strands across 4 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 | 402-406 | 5 | |
| α-helix | 413-422 | 10 | |
| α-helix | 431-450 | 20 | |
| α-helix | 451-453 | 3 | |
| β-strand | 454-455 | 2 | 1 |
| β-strand | 460-461 | 2 | 1 |
| β-strand | 462 | 1 | 2 |
| β-strand | 468 | 1 | 2 |
| α-helix | 482-495 | 14 | |
| α-helix | 500-511 | 12 | |
| α-helix | 516-518 | 3 | |
| α-helix | 522-543 | 22 | |
| α-helix | 545-550 | 6 | |
| α-helix | 552-555 | 4 | |
| α-helix | 557-568 | 12 | |
| α-helix | 569-571 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 402-406 | 5 | |
| α-helix | 413-422 | 10 | |
| α-helix | 431-449 | 19 | |
| α-helix | 450-453 | 4 | |
| β-strand | 454-455 | 2 | 3 |
| β-strand | 460-461 | 2 | 3 |
| α-helix | 474-477 | 4 | |
| α-helix | 481-495 | 15 | |
| α-helix | 500-511 | 12 | |
| α-helix | 522-543 | 22 | |
| α-helix | 549-555 | 7 | |
| α-helix | 557-568 | 12 | |
| α-helix | 570-573 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 402-406 | 5 | |
| α-helix | 413-421 | 9 | |
| α-helix | 426-428 | 3 | |
| α-helix | 431-449 | 19 | |
| α-helix | 451-453 | 3 | |
| β-strand | 462-463 | 2 | 4 |
| β-strand | 467-468 | 2 | 4 |
| α-helix | 482-493 | 12 | |
| α-helix | 500-512 | 13 | |
| α-helix | 516-518 | 3 | |
| α-helix | 522-543 | 22 | |
| α-helix | 549-555 | 7 | |
| α-helix | 557-568 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 403-409 | 7 | |
| α-helix | 415-422 | 8 | |
| α-helix | 431-449 | 19 | |
| α-helix | 450-452 | 3 | |
| α-helix | 461 | 1 | |
| β-strand | 462-463 | 2 | 5 |
| β-strand | 467-468 | 2 | 5 |
| α-helix | 474-477 | 4 | |
| α-helix | 481-495 | 15 | |
| α-helix | 500-511 | 12 | |
| α-helix | 516-518 | 3 | |
| α-helix | 522-543 | 22 | |
| α-helix | 549-568 | 20 | |
| α-helix | 570-573 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Orphan nuclear receptor NR1D2 | A, B, C, D | protein | 194 | HOMO SAPIENS | Q14995 (AlphaFold model) |
>2V0V_1 ORPHAN NUCLEAR RECEPTOR NR1D2 (chains A, B, C, D) MSKSPYVDPHKSGHEIWEEFSMSFTPAVKEVVEFAKRIPGFRDLSQHDQVNLLKAGTFEV LMVRFASLFDAKERTVTFLGSKKYSVDDLHSMGAGDLLNSMFEFSEKLNALQLSDEEMSL FTAVVLVSADRSGIENVNSVEALQETLIRALRTLIMKNHPNEASIFTKLLLKLPDLRSLN NMHSEELLAFKVHP
Structural Insight Into the Constitutive Repression Function of the Nuclear Receptor Rev-Erbbeta. Woo, E.-J., Jeong, D.G., Lim, M.-Y. et al. J Mol Biol (2007) 373:735. DOI 10.1016/J.JMB.2007.08.037 · PubMed
Other PDB entries of the same protein (UniProt Q14995 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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