Fluorine in PDB 2ngr: Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap.

The structure of Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap., PDB code: 2ngr was solved by N.Nassar, G.Hoffman, J.Clardy, R.Cerione, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.820, 67.690, 131.060, 90.00, 90.00, 90.00
R / Rfree (%)	25.3 / 29.3

The structure of Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap. also contains other interesting chemical elements:

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

The binding sites of Fluorine atom in the Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap. (pdb code 2ngr). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap., PDB code: 2ngr:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap. within 5.0Å range: probe atom residue distance (Å) B Occ A:F200 b:24.6 occ:1.00 F1 A:AF3200 0.0 24.6 1.0 AL A:AF3200 1.9 23.1 1.0 OH A:TYR32 2.3 36.3 1.0 O3B A:GDP198 2.6 16.2 1.0 O A:HOH509 3.0 29.3 1.0 NE2 A:GLN61 3.1 28.4 1.0 F2 A:AF3200 3.2 24.4 1.0 F3 A:AF3200 3.2 22.5 1.0 N A:ALA13 3.3 24.5 1.0 CZ A:TYR32 3.4 40.0 1.0 CA A:GLY12 3.6 19.8 1.0 CE1 A:TYR32 3.7 39.1 1.0 CB A:PRO34 3.7 28.2 1.0 CA A:PRO34 3.8 30.0 1.0 C A:GLY12 3.9 24.4 1.0 CD A:GLN61 4.1 28.7 1.0 PB A:GDP198 4.1 17.2 1.0 CA A:ALA13 4.2 22.4 1.0 OE1 A:GLN61 4.3 28.3 1.0 CE2 A:TYR32 4.7 41.4 1.0 O B:ALA305 4.7 28.8 1.0 O2B A:GDP198 4.7 19.9 1.0 N A:THR35 4.7 28.4 1.0 O3A A:GDP198 4.7 22.7 1.0 MG A:MG199 4.7 22.5 1.0 N A:PRO34 4.8 31.2 1.0 CB A:ALA13 4.8 22.5 1.0 C A:PRO34 4.8 28.3 1.0 O A:HOH534 4.9 23.2 1.0 O1B A:GDP198 4.9 11.4 1.0 CG A:PRO34 5.0 32.5 1.0 N A:GLY12 5.0 19.8 1.0

Fluorine binding site 2 out of 3 in the Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap. within 5.0Å range: probe atom residue distance (Å) B Occ A:F200 b:24.4 occ:1.00 F2 A:AF3200 0.0 24.4 1.0 AL A:AF3200 1.8 23.1 1.0 NZ A:LYS16 2.7 15.5 1.0 N A:GLY60 2.8 21.9 1.0 O A:HOH509 2.9 29.3 1.0 O3B A:GDP198 2.9 16.2 1.0 F1 A:AF3200 3.2 24.6 1.0 F3 A:AF3200 3.2 22.5 1.0 CA A:GLY12 3.4 19.8 1.0 CE A:LYS16 3.4 17.8 1.0 CA A:GLY60 3.5 23.8 1.0 PB A:GDP198 3.8 17.2 1.0 O1B A:GDP198 3.8 11.4 1.0 O A:HOH517 3.8 21.2 1.0 C A:ALA59 3.8 24.7 1.0 O A:THR58 3.9 24.0 1.0 CA A:ALA59 4.0 23.6 1.0 N A:GLY12 4.0 19.8 1.0 N A:ALA13 4.2 24.5 1.0 O A:ASP11 4.2 22.1 1.0 O2B A:GDP198 4.2 19.9 1.0 OE1 A:GLN61 4.2 28.3 1.0 NE2 A:GLN61 4.3 28.4 1.0 C A:GLY12 4.3 24.4 1.0 MG A:MG199 4.3 22.5 1.0 C A:ASP11 4.3 18.8 1.0 O A:GLY10 4.5 18.6 1.0 C A:GLY60 4.5 23.3 1.0 CD A:GLN61 4.6 28.7 1.0 N A:GLN61 4.7 23.7 1.0 C A:THR58 4.8 24.0 1.0 CD A:LYS16 4.9 17.0 1.0 N A:ALA59 4.9 24.6 1.0 O A:ALA59 4.9 26.8 1.0 CB A:ALA59 5.0 24.1 1.0

Fluorine binding site 3 out of 3 in the Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap. within 5.0Å range: probe atom residue distance (Å) B Occ A:F200 b:22.5 occ:1.00 F3 A:AF3200 0.0 22.5 1.0 AL A:AF3200 1.9 23.1 1.0 MG A:MG199 1.9 22.5 1.0 O A:HOH509 2.4 29.3 1.0 N A:THR35 2.6 28.4 1.0 OG1 A:THR35 2.9 22.1 1.0 O A:HOH534 2.9 23.2 1.0 O A:HOH517 2.9 21.2 1.0 O3B A:GDP198 2.9 16.2 1.0 O2B A:GDP198 3.1 19.9 1.0 CB A:THR35 3.1 26.2 1.0 F1 A:AF3200 3.2 24.6 1.0 F2 A:AF3200 3.2 24.4 1.0 CA A:THR35 3.4 27.3 1.0 CA A:PRO34 3.5 30.0 1.0 C A:PRO34 3.5 28.3 1.0 PB A:GDP198 3.6 17.2 1.0 OG1 A:THR17 4.0 23.5 1.0 O A:THR35 4.0 28.3 1.0 O A:VAL33 4.2 30.4 1.0 C A:THR35 4.2 26.6 1.0 CB A:PRO34 4.4 28.2 1.0 O A:THR58 4.5 24.0 1.0 N A:PRO34 4.6 31.2 1.0 CG2 A:THR35 4.6 27.2 1.0 O1B A:GDP198 4.6 11.4 1.0 O A:PRO34 4.7 25.7 1.0 O3A A:GDP198 4.7 22.7 1.0 C A:VAL33 4.8 30.5 1.0 O2A A:GDP198 4.9 14.5 1.0 OH A:TYR32 4.9 36.3 1.0 CE1 A:TYR32 5.0 39.1 1.0 NZ A:LYS16 5.0 15.5 1.0 CA A:ALA59 5.0 23.6 1.0

N.Nassar, G.R.Hoffman, D.Manor, J.C.Clardy, R.A.Cerione. Structures of CDC42 Bound to the Active and Catalytically Compromised Forms of CDC42GAP. Nat.Struct.Biol. V. 5 1047 1998.
ISSN: ISSN 1072-8368
PubMed: 9846874
DOI: 10.1038/4156