Atomistry » Aluminium » PDB 2xzl-3wgu » 2zjy
Atomistry »
  Aluminium »
    PDB 2xzl-3wgu »
      2zjy »

Aluminium in PDB 2zjy: Structure of the K349P Mutant of Gi Alpha 1 Subunit Bound to ALF4 and Gdp

Enzymatic activity of Structure of the K349P Mutant of Gi Alpha 1 Subunit Bound to ALF4 and Gdp

All present enzymatic activity of Structure of the K349P Mutant of Gi Alpha 1 Subunit Bound to ALF4 and Gdp:
3.6.5.1;

Protein crystallography data

The structure of Structure of the K349P Mutant of Gi Alpha 1 Subunit Bound to ALF4 and Gdp, PDB code: 2zjy was solved by T.Morikawa, A.Muroya, S.Sugio, K.Wakamatsu, T.Kohno, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.78 / 2.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 79.375, 79.375, 105.297, 90.00, 90.00, 120.00
R / Rfree (%) 18.1 / 26

Other elements in 2zjy:

The structure of Structure of the K349P Mutant of Gi Alpha 1 Subunit Bound to ALF4 and Gdp also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Magnesium (Mg) 1 atom

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Structure of the K349P Mutant of Gi Alpha 1 Subunit Bound to ALF4 and Gdp (pdb code 2zjy). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Structure of the K349P Mutant of Gi Alpha 1 Subunit Bound to ALF4 and Gdp, PDB code: 2zjy:

Aluminium binding site 1 out of 1 in 2zjy

Go back to Aluminium Binding Sites List in 2zjy
Aluminium binding site 1 out of 1 in the Structure of the K349P Mutant of Gi Alpha 1 Subunit Bound to ALF4 and Gdp


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Structure of the K349P Mutant of Gi Alpha 1 Subunit Bound to ALF4 and Gdp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al356

b:2.2
occ:1.00
 AL A:ALF356 0.0 2.2 1.0
F4 A:ALF356 1.7 30.2 1.0
F3 A:ALF356 1.8 25.1 1.0
F1 A:ALF356 1.8 8.6 1.0
F2 A:ALF356 1.8 2.2 1.0
O3B A:GDP355 2.7 22.1 1.0
NE2 A:GLN204 3.1 22.9 1.0
O1B A:GDP355 3.4 19.2 1.0
PB A:GDP355 3.4 18.1 1.0
N A:GLY203 3.6 8.3 1.0
NZ A:LYS46 3.6 4.1 1.0
MG A:MG357 3.7 2.6 1.0
N A:GLU43 3.7 8.0 1.0
NH2 A:ARG178 3.9 12.7 1.0
O2B A:GDP355 4.0 28.6 1.0
O A:HOH533 4.0 2.2 1.0
CE A:LYS46 4.2 16.7 1.0
CA A:GLY42 4.2 12.9 1.0
CD A:GLN204 4.3 21.8 1.0
CA A:GLY202 4.3 10.4 1.0
CA A:GLY203 4.4 11.0 1.0
C A:GLY202 4.4 7.8 1.0
C A:GLY42 4.5 11.3 1.0
N A:THR181 4.5 16.8 1.0
CB A:THR181 4.5 12.9 1.0
O A:THR181 4.6 25.8 1.0
CA A:GLU43 4.6 6.8 1.0
O A:ALA41 4.6 12.8 1.0
O A:VAL201 4.6 6.8 1.0
OE1 A:GLN204 4.7 15.4 1.0
O3A A:GDP355 4.8 22.1 1.0
OG1 A:THR181 5.0 18.5 1.0

Reference:

T.Morikawa, A.Muroya, S.Sugio, K.Wakamatsu, T.Kohno. How Gpcrs Activate G Proteins: Structural Changes Form C-Terminal Tail to Gdp Binding Pocket To Be Published.
Page generated: Sun Jul 6 21:44:26 2025

Last articles

Cl in 6AXR
Cl in 6AWQ
Cl in 6AWO
Cl in 6AWU
Cl in 6AWS
Cl in 6AWP
Cl in 6AW5
Cl in 6AWN
Cl in 6AV7
Cl in 6AV6
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy