Fluorine in PDB 4gs0: Crystal Structure of SHP1 Catalytic Domain with JAK1 Activation Loop Peptide

All present enzymatic activity of Crystal Structure of SHP1 Catalytic Domain with JAK1 Activation Loop Peptide:
2.7.10.2; 3.1.3.48;

The structure of Crystal Structure of SHP1 Catalytic Domain with JAK1 Activation Loop Peptide, PDB code: 4gs0 was solved by N.L.Alicea-Velazquez, J.Jakoncic, T.J.Boggon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.02 / 1.80
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	43.935, 43.935, 258.112, 90.00, 90.00, 120.00
R / Rfree (%)	16.2 / 19.5

The binding sites of Fluorine atom in the Crystal Structure of SHP1 Catalytic Domain with JAK1 Activation Loop Peptide (pdb code 4gs0). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of SHP1 Catalytic Domain with JAK1 Activation Loop Peptide, PDB code: 4gs0:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of SHP1 Catalytic Domain with JAK1 Activation Loop Peptide


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 SHP1 Catalytic Domain with JAK1 Activation Loop Peptide within 5.0Å range: probe atom residue distance (Å) B Occ C:F3 b:57.7 occ:0.87 F1 C:FTY3 0.0 57.7 0.9 C1 C:FTY3 1.3 54.0 0.9 F2 C:FTY3 2.2 53.1 0.9 CZ C:FTY3 2.3 52.5 0.9 P C:FTY3 2.6 45.6 0.9 CE1 C:FTY3 2.8 51.3 0.9 O3P C:FTY3 3.1 45.2 0.9 O1P C:FTY3 3.2 46.4 0.9 O B:HOH667 3.3 39.3 1.0 CE2 C:FTY3 3.4 47.2 0.9 O2P C:FTY3 3.9 44.9 0.9 CD1 C:FTY3 4.1 52.6 0.9 CD2 C:FTY3 4.6 47.7 0.9 CB C:UNK4 4.8 70.5 1.0 CG C:FTY3 4.9 48.2 0.9 NH2 B:ARG459 4.9 42.5 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of SHP1 Catalytic Domain with JAK1 Activation Loop Peptide


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of SHP1 Catalytic Domain with JAK1 Activation Loop Peptide within 5.0Å range: probe atom residue distance (Å) B Occ C:F3 b:53.1 occ:0.87 F2 C:FTY3 0.0 53.1 0.9 C1 C:FTY3 1.4 54.0 0.9 F1 C:FTY3 2.2 57.7 0.9 CZ C:FTY3 2.3 52.5 0.9 CE2 C:FTY3 2.6 47.2 0.9 P C:FTY3 2.6 45.6 0.9 O2P C:FTY3 3.1 44.9 0.9 O3P C:FTY3 3.1 45.2 0.9 CA B:GLY458 3.4 30.6 1.0 CG B:GLN500 3.4 47.1 1.0 O B:HOH667 3.5 39.3 1.0 CE1 C:FTY3 3.6 51.3 0.9 N B:GLY458 3.6 28.7 1.0 CB B:GLN500 3.7 44.9 1.0 O1P C:FTY3 3.9 46.4 0.9 CD2 C:FTY3 4.0 47.7 0.9 CG1 B:ILE457 4.3 28.7 1.0 CD B:GLN500 4.5 50.9 1.0 C B:GLY458 4.6 29.6 1.0 OE1 B:GLN500 4.6 60.6 1.0 CD1 C:FTY3 4.7 52.6 0.9 N B:ARG459 4.8 27.3 1.0 C B:ILE457 4.8 25.8 1.0 CG C:FTY3 4.9 48.2 0.9 NE2 B:GLN504 4.9 35.7 1.0 CD1 B:ILE457 5.0 31.6 1.0

N.L.Alicea-Velazquez, J.Jakoncic, T.J.Boggon. Structure-Guided Studies of the Shp-1/JAK1 Interaction Provide New Insights Into Phosphatase Catalytic Domain Substrate Recognition. J.Struct.Biol. V. 181 243 2013.
ISSN: ISSN 1047-8477
PubMed: 23296072
DOI: 10.1016/J.JSB.2012.12.009