X-ray diffraction
2.9Å resolution

Crystal Structure of Hormone Receptor

Source organism: Homo sapiens

Function and Biology Details

Reactions catalysed:
L-arginine + 2-oxoglutarate + O(2) = (3S)-3-hydroxy-L-arginine + succinate + CO(2)
(1a) S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-N(omega)-methyl-L-arginine
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Cinnamaldehyde + CoA + NADP(+) = cinnamoyl-CoA + NADPH
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate
NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone
A (3R)-3-hydroxyacyl-[acyl-carrier-protein] + a UDP-3-O-((3R)-hydroxyacyl)-alpha-D-glucosamine = a UDP-2-N,3-O-bis((3R)-3-hydroxyacyl)-alpha-D-glucosamine + a holo-[acyl-carrier-protein]
Succinate + a quinone = fumarate + a quinol
N-acetyl-O-acetylneuraminate + H(2)O = N-acetylneuraminate + acetate
N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
NTP + H(2)O = NDP + phosphate
UDP-alpha-D-glucose = UDP-alpha-D-galactose
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
5'-deoxyadenosine + H(2)O = 5-deoxy-D-ribose + adenine
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine(2552) in 23S rRNA
A beta-lactam + H(2)O = a substituted beta-amino acid
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
(1a) L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Atrial natriuretic peptide receptor 3 Chain: A
Molecule details ›
Chain: A
Length: 441 amino acids
Theoretical weight: 49.54 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
  • Canonical: P17342 (Residues: 44-485; Coverage: 86%)
Gene names: ANPRC, C5orf23, NPR3, NPRC
Sequence domains: Receptor family ligand binding region
Structure domains: Rossmann fold

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, NDG, BMA, MAN
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P6122
Unit cell:
a: 217.189Å b: 217.189Å c: 130.793Å
α: 90° β: 90° γ: 120°
R R work R free
0.243 0.243 0.256
Expression system: Drosophila melanogaster