4PLE: Nuclear receptor subfamily 5 group A member 2
Human Nuclear Receptor Liver Receptor Homologue-1, LRH-1, Bound to an E. Coli Phospholipid and a Fragment of TIF-2. Determined by X-ray diffraction at 1.75 Å resolution. Released 16 Dec 2015.
- Method
- X-ray diffraction
- Resolution
- 1.75 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 9,019
- Mol. weight
- 130.14 kDa
- Ligands
- EPH, CPS
- Released
- 16 Dec 2015
Explore 4PLE in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4PLE contains 65 α-helices and 8 β-strands across 8 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.
Chain A: 15 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 303-310 | 8 | |
| α-helix | 315-331 | 17 | |
| α-helix | 335-337 | 3 | |
| α-helix | 341-362 | 22 | |
| α-helix | 366-368 | 3 | |
| α-helix | 371-397 | 27 | |
| β-strand | 402-404 | 3 | 1 |
| α-helix | 409 | 1 | |
| β-strand | 410-412 | 3 | 1 |
| α-helix | 413-419 | 7 | |
| α-helix | 422-440 | 19 | |
| α-helix | 445-456 | 12 | |
| α-helix | 467-488 | 22 | |
| α-helix | 495-500 | 6 | |
| α-helix | 503-522 | 20 | |
| α-helix | 527 | 1 | |
| α-helix | 531-537 | 7 | |
Chains B and D: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 743-748 | 6 | |
Chain C: 16 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 303-310 | 8 | |
| α-helix | 315-331 | 17 | |
| α-helix | 335-337 | 3 | |
| α-helix | 338-340 | 3 | |
| α-helix | 341-362 | 22 | |
| α-helix | 366-368 | 3 | |
| α-helix | 371-397 | 27 | |
| β-strand | 402-404 | 3 | 2 |
| α-helix | 405 | 1 | |
| β-strand | 410-412 | 3 | 2 |
| α-helix | 413-419 | 7 | |
| α-helix | 422-440 | 19 | |
| α-helix | 445-456 | 12 | |
| α-helix | 467-488 | 22 | |
| α-helix | 495-500 | 6 | |
| α-helix | 503-522 | 20 | |
| α-helix | 527 | 1 | |
| α-helix | 531-537 | 7 | |
Chain E: 15 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 303-310 | 8 | |
| α-helix | 315-331 | 17 | |
| α-helix | 335-337 | 3 | |
| α-helix | 338-340 | 3 | |
| α-helix | 341-361 | 21 | |
| α-helix | 366-368 | 3 | |
| α-helix | 371-397 | 27 | |
| β-strand | 402-404 | 3 | 3 |
| α-helix | 409 | 1 | |
| β-strand | 410-412 | 3 | 3 |
| α-helix | 413-419 | 7 | |
| α-helix | 422-440 | 19 | |
| α-helix | 445-456 | 12 | |
| α-helix | 467-488 | 22 | |
| α-helix | 495-500 | 6 | |
| α-helix | 503-522 | 20 | |
| α-helix | 532-536 | 5 | |
Chains F and H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 743-750 | 8 | |
Chain G: 15 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 303-310 | 8 | |
| α-helix | 315-331 | 17 | |
| α-helix | 335-337 | 3 | |
| α-helix | 338-340 | 3 | |
| α-helix | 341-362 | 22 | |
| α-helix | 366-368 | 3 | |
| α-helix | 371-397 | 27 | |
| β-strand | 402-404 | 3 | 4 |
| α-helix | 409 | 1 | |
| β-strand | 410-412 | 3 | 4 |
| α-helix | 413-419 | 7 | |
| α-helix | 422-440 | 19 | |
| α-helix | 445-456 | 12 | |
| α-helix | 467-488 | 22 | |
| α-helix | 495-500 | 6 | |
| α-helix | 503-522 | 20 | |
| α-helix | 532-537 | 6 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Nuclear receptor subfamily 5 group A member 2 | A, C, E, G | protein | 245 | Homo sapiens | O00482 (AlphaFold model) |
| Nuclear receptor coactivator 2 | B, D, F, H | protein | 14 | Homo sapiens | Q15596 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>4PLE_1 Nuclear receptor subfamily 5 group A member 2 (chains A, C, E, G)
AAASIPHLILELLKCEPDEPQVQAKIMAYLQQEQANRSKHEKLSTFGLMCKMADQTLFSI
VEWARSSIFFRELKVDDQMKLLQNCWSELLILDHIYRQVVHGKEGSIFLVTGQQVDYSII
ASQAGATLNNLMSHAQELVAKLRSLQFDQREFVCLKFLVLFSLDVKNLENFQLVEGVQEQ
VNAALLDYTMCNYPQQTEKFGQLLLRLPEIRAISMQAEEYLYYKHLNGDVPYNNLLIEML
HAKRA
Sequence of entity 2 (B, D, F, H), FASTA
>4PLE_2 Nuclear receptor coactivator 2 (chains B, D, F, H)
KENALLRYLLDKDD
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| EPH | L-alpha-phosphatidyl-beta-oleoyl-gamma-palmitoyl-phosphatidylethanolamine | C39 H68 N O8 P | 4 |
| CPS | 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate | C32 H58 N2 O7 S | 12 |
Primary citation
Unexpected Allosteric Network Contributes to LRH-1 Co-regulator Selectivity. Musille, P.M., Kossmann, B.R., Kohn, J.A. et al. J Biol Chem (2016) 291:1411-1426. DOI 10.1074/jbc.M115.662874 · PubMed
Other PDB entries of the same protein (UniProt O00482 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6VC2 1.7 Å, LRH-1 bound to SS-RJW100 and a fragment of the Tif2 Coactivator
- 3PLZ 1.75 Å, Human LRH1 LBD bound to GR470
- 4PLD 1.75 Å, Human Nuclear Receptor Liver Receptor Homologue-1, LRH-1, in its apo State Bound to a…
- 4ONI 1.8 Å, Structure of Human Orphan Receptor LRH1 bound to two bacterial phospholipids
- 5L11 1.85 Å, Human Liver Receptor Homologue-1 (LRH-1) Bound to RJW100 and a Fragment of TIF-2
- 4RWV 1.86 Å, Crystal structure of PIP3 bound human nuclear receptor LRH-1 (Liver Receptor Homolog 1,…
- 1YUC 1.9 Å, Human Nuclear Receptor Liver Receptor Homologue-1, LRH-1, Bound to Phospholipid and a…
- 4DOR 1.9 Å, Human Nuclear Receptor Liver Receptor Homologue-1, LRH-1, in its apo State Bound to a…
- 5SYZ 1.93 Å, Human Liver Receptor Homologue-1 (LRH-1) Bound to a RJW100 stereoisomer and a Fragment…
- 5UNJ 1.96 Å, Structure of Human Liver Receptor Homolog 1 in complex with PGC1a and RJW100
- 4DOS 2.0 Å, Human Nuclear Receptor Liver Receptor Homologue-1, LRH-1, Bound to DLPC and a Fragment…
- 6OQX 2.0 Å, Human Liver Receptor Homolog-1 bound to the agonist 5N and a fragment of the Tif2…
Browse structure collections
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