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

Protein crystallography data

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

Other elements in 5c2k:

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

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

Magnesium Binding Sites:

The binding sites of Magnesium 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 Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Fusion Protein Linked By Rhoa and the Gap Domain of Mgcracgap, PDB code: 5c2k:

Magnesium binding site 1 out of 1 in 5c2k

Go back to Magnesium Binding Sites List in 5c2k
Magnesium binding site 1 out of 1 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 Magnesium with other atoms in the Mg 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:Mg501

b:9.6
occ:1.00
O2B A:GDP503 2.0 10.1 1.0
OG1 A:THR19 2.0 10.3 1.0
O A:HOH695 2.1 9.6 1.0
O A:HOH753 2.1 10.4 1.0
F3 A:AF3502 2.1 10.5 1.0
OG1 A:THR37 2.1 10.4 1.0
CB A:THR37 3.1 9.9 1.0
CB A:THR19 3.1 9.3 1.0
PB A:GDP503 3.3 9.6 1.0
O1B A:GDP503 3.5 11.2 1.0
AL A:AF3502 3.6 9.1 1.0
N A:THR37 3.8 10.4 1.0
N A:THR19 3.9 9.6 1.0
OD2 A:ASP59 4.0 12.2 1.0
CA A:THR37 4.1 9.9 1.0
CA A:THR19 4.1 10.9 1.0
O1A A:GDP503 4.1 10.1 1.0
OD1 A:ASP59 4.2 11.4 1.0
CG2 A:THR19 4.2 12.0 1.0
CG2 A:THR37 4.2 10.4 1.0
O3B A:GDP503 4.3 8.8 1.0
O A:HOH680 4.3 15.8 1.0
O3A A:GDP503 4.3 9.0 1.0
CG A:ASP59 4.4 11.8 1.0
F2 A:AF3502 4.5 10.1 1.0
PA A:GDP503 4.5 9.8 1.0
NH2 A:ARG247 4.6 10.3 1.0
O A:THR60 4.6 10.9 1.0
O2A A:GDP503 4.6 10.6 1.0
O A:HOH697 4.7 10.0 1.0
O A:VAL35 4.7 12.6 1.0
C A:PRO36 4.8 10.9 1.0
CB A:LYS18 4.9 9.8 1.0
F1 A:AF3502 4.9 11.4 1.0
C A:LYS18 5.0 8.8 1.0
O A:HOH638 5.0 19.7 1.0

Reference:

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.
Page generated: Mon Dec 14 20:05:22 2020

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