Fluorine in PDB 5c2k: Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap

The structure of Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap, PDB code: 5c2k was solved by K.Murayama, M.Kato-Murayama, T.Hosaka, T.Kitamura, S.Yokoyama, M.Shirouzu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.26 / 1.42
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.491, 77.041, 62.253, 90.00, 108.53, 90.00
R / Rfree (%)	18.4 / 20.6

The structure of Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Aluminium	(Al)	1 atom

The binding sites of Fluorine atom in the Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap (pdb code 5c2k). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap, PDB code: 5c2k:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap


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 Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:11.4 occ:1.00 F1 A:AF3502 0.0 11.4 1.0 AL A:AF3502 1.7 9.1 1.0 O1B A:GDP503 2.6 11.2 1.0 NE A:ARG247 2.7 10.4 1.0 O A:HOH697 2.8 10.0 1.0 NE2 A:GLN63 2.9 10.6 1.0 F2 A:AF3502 3.0 10.1 1.0 F3 A:AF3502 3.1 10.5 1.0 NH2 A:ARG247 3.2 10.3 1.0 N A:ALA15 3.3 9.8 1.0 CZ A:ARG247 3.4 9.9 1.0 CG A:ARG247 3.6 10.5 1.0 CB A:PRO36 3.6 12.5 1.0 CD A:ARG247 3.7 10.5 1.0 CA A:GLY14 3.7 10.2 1.0 CD A:GLN63 3.8 10.8 1.0 CA A:PRO36 3.8 11.7 1.0 OE1 A:GLN63 3.9 10.5 1.0 C A:GLY14 4.0 10.2 1.0 PB A:GDP503 4.2 9.6 1.0 CA A:ALA15 4.2 10.7 1.0 N A:THR37 4.5 10.4 1.0 NH1 A:ARG247 4.7 11.0 1.0 CB A:ALA15 4.7 11.4 1.0 O A:ARG247 4.7 13.0 1.0 C A:PRO36 4.7 10.9 1.0 O3A A:GDP503 4.9 9.0 1.0 O2B A:GDP503 4.9 10.1 1.0 N A:PRO36 4.9 11.4 1.0 MG A:MG501 4.9 9.6 1.0 O3B A:GDP503 5.0 8.8 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap


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 the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:10.1 occ:1.00 F2 A:AF3502 0.0 10.1 1.0 AL A:AF3502 1.7 9.1 1.0 NZ A:LYS18 2.7 9.6 1.0 N A:GLY62 2.8 9.2 1.0 O1B A:GDP503 2.9 11.2 1.0 O A:HOH697 2.9 10.0 1.0 F1 A:AF3502 3.0 11.4 1.0 F3 A:AF3502 3.0 10.5 1.0 CA A:GLY14 3.4 10.2 1.0 CE A:LYS18 3.5 10.8 1.0 CA A:GLY62 3.5 11.9 1.0 C A:ALA61 3.8 11.4 1.0 PB A:GDP503 3.9 9.6 1.0 O3B A:GDP503 3.9 8.8 1.0 N A:ALA15 3.9 9.8 1.0 O A:THR60 4.0 10.9 1.0 CA A:ALA61 4.0 11.2 1.0 O A:HOH695 4.0 9.6 1.0 N A:GLY14 4.1 10.8 1.0 NE2 A:GLN63 4.1 10.6 1.0 OE1 A:GLN63 4.2 10.5 1.0 O A:ASP13 4.2 10.1 1.0 C A:GLY14 4.2 10.2 1.0 O2B A:GDP503 4.4 10.1 1.0 C A:ASP13 4.4 10.0 1.0 O A:GLY12 4.5 9.8 1.0 C A:GLY62 4.5 11.4 1.0 CD A:GLN63 4.5 10.8 1.0 MG A:MG501 4.5 9.6 1.0 N A:GLN63 4.6 10.9 1.0 C A:THR60 4.8 10.2 1.0 N A:ALA61 4.9 10.8 1.0 CD A:LYS18 4.9 10.6 1.0 O A:ALA61 4.9 13.1 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:10.5 occ:1.00 F3 A:AF3502 0.0 10.5 1.0 AL A:AF3502 1.8 9.1 1.0 MG A:MG501 2.1 9.6 1.0 O1B A:GDP503 2.7 11.2 1.0 O A:HOH697 2.7 10.0 1.0 N A:THR37 2.8 10.4 1.0 O A:HOH695 2.9 9.6 1.0 O A:HOH753 3.0 10.4 1.0 OG1 A:THR37 3.0 10.4 1.0 O2B A:GDP503 3.0 10.1 1.0 F2 A:AF3502 3.0 10.1 1.0 F1 A:AF3502 3.1 11.4 1.0 CB A:THR37 3.2 9.9 1.0 PB A:GDP503 3.5 9.6 1.0 CA A:THR37 3.5 9.9 1.0 C A:PRO36 3.7 10.9 1.0 CA A:PRO36 3.7 11.7 1.0 NH2 A:ARG247 3.9 10.3 1.0 O A:THR37 4.1 10.9 1.0 OG1 A:THR19 4.1 10.3 1.0 C A:THR37 4.3 10.2 1.0 O A:THR60 4.3 10.9 1.0 O3B A:GDP503 4.4 8.8 1.0 CB A:PRO36 4.5 12.5 1.0 O A:VAL35 4.6 12.6 1.0 O3A A:GDP503 4.6 9.0 1.0 CG2 A:THR37 4.6 10.4 1.0 NZ A:LYS18 4.8 9.6 1.0 CZ A:ARG247 4.8 9.9 1.0 O1A A:GDP503 4.8 10.1 1.0 O A:PRO36 4.9 13.3 1.0 NE A:ARG247 4.9 10.4 1.0 CA A:ALA61 4.9 11.2 1.0 N A:PRO36 5.0 11.4 1.0

K.Murayama, M.Kato-Murayama, T.Hosaka, T.Kawashima, T.Kitamura, S.Yokoyama, M.Shirouzu. Structural Basis of G-Protein Target Alternation of Mgcracgap By Phospholylation To Be Published.