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Fluorine in PDB 3mnp: Crystal Structure of the Agonist Form of Mouse Glucocorticoid Receptor Stabilized By (A611V, V708A, E711G) Mutations at 1.50A

Protein crystallography data

The structure of Crystal Structure of the Agonist Form of Mouse Glucocorticoid Receptor Stabilized By (A611V, V708A, E711G) Mutations at 1.50A, PDB code: 3mnp was solved by G.A.Schoch, T.Seitz, J.Benz, D.Banner, M.Stihle, B.D'arcy, R.Thoma, R.Sterner, M.Hennig, A.Ruf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.38 / 1.50
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 72.089, 72.089, 128.827, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 20.1

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of the Agonist Form of Mouse Glucocorticoid Receptor Stabilized By (A611V, V708A, E711G) Mutations at 1.50A (pdb code 3mnp). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of the Agonist Form of Mouse Glucocorticoid Receptor Stabilized By (A611V, V708A, E711G) Mutations at 1.50A, PDB code: 3mnp:

Fluorine binding site 1 out of 1 in 3mnp

Go back to Fluorine Binding Sites List in 3mnp
Fluorine binding site 1 out of 1 in the Crystal Structure of the Agonist Form of Mouse Glucocorticoid Receptor Stabilized By (A611V, V708A, E711G) Mutations at 1.50A


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of the Agonist Form of Mouse Glucocorticoid Receptor Stabilized By (A611V, V708A, E711G) Mutations at 1.50A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F784

b:13.6
occ:1.00
F1 A:DEX784 0.0 13.6 1.0
C9 A:DEX784 1.3 13.8 1.0
C11 A:DEX784 2.3 14.3 1.0
C8 A:DEX784 2.3 13.6 1.0
C10 A:DEX784 2.4 14.6 1.0
C5 A:DEX784 2.8 12.3 1.0
C7 A:DEX784 2.8 14.4 1.0
C1 A:DEX784 2.9 16.9 1.0
C12 A:DEX784 2.9 13.8 1.0
C14 A:DEX784 2.9 13.0 1.0
C6 A:DEX784 3.3 14.0 1.0
CE2 A:PHE629 3.4 17.9 1.0
C13 A:DEX784 3.5 13.3 1.0
C2 A:DEX784 3.6 19.3 1.0
O2 A:DEX784 3.6 14.6 1.0
C4 A:DEX784 3.6 15.6 1.0
C19 A:DEX784 3.7 16.5 1.0
CB A:LEU569 3.9 15.4 1.0
SD A:MET652 3.9 18.9 1.0
C3 A:DEX784 3.9 22.4 1.0
CD1 A:LEU569 4.1 17.9 1.0
CD2 A:PHE629 4.1 19.8 1.0
CZ A:PHE629 4.2 17.6 1.0
C15 A:DEX784 4.3 12.9 1.0
O3 A:DEX784 4.4 15.1 1.0
CG A:LEU569 4.5 17.8 1.0
C17 A:DEX784 4.6 13.3 1.0
C18 A:DEX784 4.7 14.9 1.0
O A:LEU569 4.7 16.1 1.0
C A:LEU569 4.9 17.4 1.0
CA A:LEU569 4.9 16.0 1.0
CD2 A:LEU569 4.9 20.1 1.0
O1 A:DEX784 5.0 24.3 1.0

Reference:

T.Seitz, R.Thoma, G.A.Schoch, M.Stihle, J.Benz, B.D'arcy, A.Wiget, A.Ruf, M.Hennig, R.Sterner. Enhancing the Stability and Solubility of the Glucocorticoid Receptor Ligand-Binding Domain By High-Throughput Library Screening. J.Mol.Biol. V. 403 562 2010.
ISSN: ISSN 0022-2836
PubMed: 20850457
DOI: 10.1016/J.JMB.2010.08.048
Page generated: Wed Jul 31 20:43:08 2024

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