Magnesium 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:

Fluorine	(F)	3 atoms
Aluminium	(Al)	1 atom

The binding sites of Magnesium 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 Magnesium atom.
In total only one binding site of Magnesium was 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:

Magnesium binding site 1 out of 1 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 Magnesium with other atoms in the Mg 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:Mg199 b:22.5 occ:1.00 F3 A:AF3200 1.9 22.5 1.0 O2B A:GDP198 2.0 19.9 1.0 OG1 A:THR17 2.1 23.5 1.0 O A:HOH517 2.1 21.2 1.0 OG1 A:THR35 2.2 22.1 1.0 O A:HOH534 2.2 23.2 1.0 CB A:THR35 3.1 26.2 1.0 PB A:GDP198 3.2 17.2 1.0 CB A:THR17 3.3 18.3 1.0 AL A:AF3200 3.4 23.1 1.0 O3B A:GDP198 3.4 16.2 1.0 N A:THR35 3.6 28.4 1.0 CA A:THR35 4.0 27.3 1.0 OD2 A:ASP57 4.0 25.6 1.0 N A:THR17 4.0 15.3 1.0 O2A A:GDP198 4.2 14.5 1.0 O3A A:GDP198 4.2 22.7 1.0 CA A:THR17 4.2 19.2 1.0 CG2 A:THR35 4.2 27.2 1.0 O A:HOH509 4.2 29.3 1.0 O1B A:GDP198 4.3 11.4 1.0 F2 A:AF3200 4.3 24.4 1.0 CG2 A:THR17 4.3 18.5 1.0 O A:VAL33 4.4 30.4 1.0 O A:HOH573 4.5 29.0 1.0 PA A:GDP198 4.5 17.1 1.0 OD1 A:ASP57 4.6 23.6 1.0 O A:THR58 4.7 24.0 1.0 CG A:ASP57 4.7 27.4 1.0 C A:PRO34 4.7 28.3 1.0 O1A A:GDP198 4.7 21.0 1.0 F1 A:AF3200 4.7 24.6 1.0 CA A:PRO34 4.8 30.0 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