› 3v3q

X-ray diffraction
2.22Å resolution

Crystal Structure of Human Nur77 Ligand-binding Domain in Complex with Ethyl 2-[2,3,4 trimethoxy-6(1-octanoyl)phenyl]acetate

Released:
DOI: 10.2210/pdb3v3q/pdb
PDB entry 3v3q coloured by chain, front view.
PDB entry 3v3q coloured by chain, side view.
PDB entry 3v3q coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The orphan nuclear receptor Nur77 regulates LKB1 localization and activates AMPK.
Zhan YY, Chen Y, Zhang Q, Zhuang JJ, Tian M, Chen HZ, Zhang LR, Zhang HK, He JP, Wang WJ, Wu R, Wang Y, Shi C, Yang K, Li AZ, Xin YZ, Li TY, Yang JY, Zheng ZH, Yu CD, Lin SC, Chang C, Huang PQ, Lin T, Wu Q
Nat Chem Biol 8 897-904 (2012)
PMID: 22983157

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-540298 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclear receptor subfamily 4immunitygroup A member 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 257 amino acids
Theoretical weight: 28.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22736 (Residues: 351-598; Coverage: 42%)
Gene names: GFRP1, HMR, NAK1, NR4A1
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

3 bound ligands:
Ligand TMY 2 x TMY
Ligand GOL 4 x GOL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 74.242Å b: 76.773Å c: 129.193Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.209 0.286
Expression system: Escherichia coli

Quick links

Citations

17 review citations

AMP-activated protein kinase: a target for old drugs against diabetes and cancer.
Russo et al. (2013)
16 more

10 mentions without citation

Assessment of NR4A Ligands That Directly Bind and Modulate the Orphan Nuclear Receptor Nurr1.
Munoz-Tello et al. (2020)
9 more