6HL0: Bile acid receptor

Crystal Structure of Farnesoid X receptor (FXR) with bound NCoA-2 peptide. Determined by X-ray diffraction at 1.66 Å resolution. Released 29 May 2019.

Method: X-ray diffraction
Resolution: 1.66 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,153
Mol. weight: 28.75 kDa
Released: 29 May 2019

Explore 6HL0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6HL0 contains 15 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.

Chain A: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	247-262	16
α-helix	267-275	9
α-helix	280-303	24
α-helix	308-310	3
α-helix	313-334	22
α-helix	335-339	5
α-helix	344-352	9
α-helix	359-374	16
α-helix	379-390	12
α-helix	401-422	22
α-helix	429-452	24
α-helix	456-458	3
α-helix	459-462	4
α-helix	463-468	6

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	743-749	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bile acid receptor	A	protein	232	Homo sapiens	Q96RI1 (AlphaFold model)
NCoA-2 peptide (Nuclear receptor coactivator 2), LYS-GLU-ASN-ALA-LEU-LEU-ARG-TYR-LEU-LEU-ASP-LYS-ASP	B	protein	13	Homo sapiens

Sequence of entity 1 (A), FASTA

>6HL0_1 Bile acid receptor (chains A)
SHMELTPDQQTLLHFIMDSYNKQRMPQEITNKILKEEFSAEENFLILTEMATNHVQVLVE
FTKKLPGFQTLDHEDQIALLKGSAVEAMFLRSAEIFNKKLPSGHSDLLEERIRNSGISDE
YITPMFSFYKSIGELKMTQEEYALLTAIVILSPDRQYIKDREAVEKLQEPLLDVLQKLCK
IHQPENPQHFACLLGRLTELRTFNHHHAEMLMSWRVNDHKFTPLLCEIWDVQ

Sequence of entity 2 (B), FASTA

>6HL0_2 NCoA-2 peptide (Nuclear receptor coactivator 2), LYS-GLU-ASN-ALA-LEU-LEU-ARG-TYR-LEU-LEU-ASP-LYS-ASP (chains B)
KENALLRYLLDKD

Primary citation

Molecular tuning of farnesoid X receptor partial agonism. Merk, D., Sreeramulu, S., Kudlinzki, D. et al. Nat Commun (2019) 10:2915-2915. DOI 10.1038/s41467-019-10853-2 · PubMed

Other PDB entries of the same protein (UniProt Q96RI1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6HL1 1.6 Å, Crystal Structure of Farnesoid X receptor (FXR) with bound NCoA-2 peptide and CDCA
4OIV 1.7 Å, Structural basis for small molecule NDB as a selective antagonist of FXR
5Q0I 1.7 Å, Ligand binding to FARNESOID-X-RECEPTOR
1OSH 1.8 Å, A Chemical, Genetic, and Structural Analysis of the nuclear bile acid receptor FXR
5Q0K 1.8 Å, Ligand binding to FARNESOID-X-RECEPTOR
5Q0P 1.8 Å, Ligand binding to FARNESOID-X-RECEPTOR
5Q14 1.85 Å, Ligand binding to FARNESOID-X-RECEPTOR
5Q1E 1.85 Å, Ligand binding to FARNESOID-X-RECEPTOR
5Q0V 1.87 Å, Ligand binding to FARNESOID-X-RECEPTOR
5Q1D 1.89 Å, Ligand binding to FARNESOID-X-RECEPTOR
3BEJ 1.9 Å, Structure of human FXR in complex with MFA-1 and co-activator peptide
3L1B 1.9 Å, Complex Structure of FXR Ligand-binding domain with a tetrahydroazepinoindole compound

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