Zinc in PDB 7uzo: Parathyroid Hormone 1 Receptor Extracellular Domain Complexed with A Peptide Ligand Containing One Beta-Amino Acid

Protein crystallography data

The structure of Parathyroid Hormone 1 Receptor Extracellular Domain Complexed with A Peptide Ligand Containing One Beta-Amino Acid, PDB code: 7uzo was solved by Z.Yu, A.T.Bruchs, C.A.Bingman, S.H.Gellman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.01 / 1.30
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 56.023, 56.023, 100.823, 90, 90, 120
R / Rfree (%) 15.7 / 18.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Parathyroid Hormone 1 Receptor Extracellular Domain Complexed with A Peptide Ligand Containing One Beta-Amino Acid (pdb code 7uzo). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Parathyroid Hormone 1 Receptor Extracellular Domain Complexed with A Peptide Ligand Containing One Beta-Amino Acid, PDB code: 7uzo:

Zinc binding site 1 out of 1 in 7uzo

Go back to Zinc Binding Sites List in 7uzo
Zinc binding site 1 out of 1 in the Parathyroid Hormone 1 Receptor Extracellular Domain Complexed with A Peptide Ligand Containing One Beta-Amino Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Parathyroid Hormone 1 Receptor Extracellular Domain Complexed with A Peptide Ligand Containing One Beta-Amino Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn101

b:15.7
occ:0.33
O B:HOH212 1.9 24.4 0.3
NE2 B:HIS26 2.0 14.2 1.0
CE1 B:HIS26 3.0 17.5 1.0
CD2 B:HIS26 3.1 13.8 1.0
HE1 B:HIS26 3.1 21.0 1.0
HD2 B:HIS26 3.3 16.5 1.0
O A:HOH301 4.0 37.2 1.0
ND1 B:HIS26 4.1 17.6 1.0
CG B:HIS26 4.2 14.2 1.0
HB3 B:PHE22 4.4 20.7 1.0
HD1 B:HIS26 4.9 21.2 1.0
O B:PHE22 4.9 16.4 1.0

Reference:

S.Liu, Z.Yu, E.J.Daley, C.A.Bingman, A.T.Bruchs, T.J.Gardella, S.H.Gellman. Altered Signaling at the Pth Receptor Via Modified Agonist Contacts with the Extracellular Domain Provides A Path to Prolonged Agonism in Vivo. Proc.Natl.Acad.Sci.Usa V. 119 36119 2022.
ISSN: ESSN 1091-6490
PubMed: 36409914
DOI: 10.1073/PNAS.2212736119
Page generated: Wed Oct 30 12:27:04 2024

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