GR in complex with desisobutyrylciclesonide. Determined by X-ray diffraction at 1.8 Å resolution. Released 25 Nov 2015.
Explore 4UDD in 3D Show helices and sheets RCSB PDB PDBe
4UDD contains 14 α-helices and 4 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 | 532-538 | 7 | |
| α-helix | 540-545 | 6 | |
| α-helix | 553-554 | 2 | |
| α-helix | 556-579 | 24 | |
| α-helix | 584-586 | 3 | |
| α-helix | 589-615 | 27 | |
| β-strand | 621-624 | 4 | 1 |
| β-strand | 627-629 | 3 | 1 |
| α-helix | 631-634 | 4 | |
| α-helix | 639-655 | 17 | |
| α-helix | 660-671 | 12 | |
| β-strand | 674-675 | 2 | 2 |
| α-helix | 683-702 | 20 | |
| α-helix | 708-741 | 34 | |
| α-helix | 743-745 | 3 | |
| α-helix | 751-765 | 15 | |
| β-strand | 770-771 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 743-750 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glucocorticoid receptor | A | protein | 280 | HOMO SAPIENS | P04150 (AlphaFold model) |
| Nuclear receptor coactivator 2 | B | protein | 14 | HOMO SAPIENS | Q15596 (AlphaFold model) |
>4UDD_1 GLUCOCORTICOID RECEPTOR (chains A) GSIQQATTGVSQETSENPGDKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSTW RIMTTLNMLGGRQMIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMSLMAFALGWRSYRQSS ANLLCFAPDLIINEQRMTLPDMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPK DGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCF QTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK
>4UDD_2 NUCLEAR RECEPTOR COACTIVATOR 2 (chains B) KENALLRYLLDKDD
| ID | Name | Formula | Copies |
|---|---|---|---|
| CV7 | Desisobuytyryl ciclesonide | C28 H38 O6 | 1 |
| CPS | 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate | C32 H58 N2 O7 S | 3 |
Water and common crystallization additives (EDO) are not listed.
Ligand Binding Mechanism in Steroid Receptors: From Conserved Plasticity to Differential Evolutionary Constraints. Edman, K., Hosseini, A., Bjursell, M.K. et al. Structure (2015) 23:2280. DOI 10.1016/J.STR.2015.09.012 · PubMed
Other PDB entries of the same protein (UniProt P04150 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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