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Chlorine in PDB 6z1d: Crystal Structure of the Aaa Domain of Rubisco Activase From Nostoc Sp. (Strain Pcc 7120), Gadolinium Complex

Protein crystallography data

The structure of Crystal Structure of the Aaa Domain of Rubisco Activase From Nostoc Sp. (Strain Pcc 7120), Gadolinium Complex, PDB code: 6z1d was solved by L.Popilka, A.Bracher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.63 / 2.71
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 111.990, 111.990, 283.818, 90.00, 90.00, 120.00
R / Rfree (%) 21.6 / 25.9

Other elements in 6z1d:

The structure of Crystal Structure of the Aaa Domain of Rubisco Activase From Nostoc Sp. (Strain Pcc 7120), Gadolinium Complex also contains other interesting chemical elements:

Gadolinium (Gd) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Aaa Domain of Rubisco Activase From Nostoc Sp. (Strain Pcc 7120), Gadolinium Complex (pdb code 6z1d). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the Aaa Domain of Rubisco Activase From Nostoc Sp. (Strain Pcc 7120), Gadolinium Complex, PDB code: 6z1d:

Chlorine binding site 1 out of 1 in 6z1d

Go back to Chlorine Binding Sites List in 6z1d
Chlorine binding site 1 out of 1 in the Crystal Structure of the Aaa Domain of Rubisco Activase From Nostoc Sp. (Strain Pcc 7120), Gadolinium Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Aaa Domain of Rubisco Activase From Nostoc Sp. (Strain Pcc 7120), Gadolinium Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl404

b:53.1
occ:1.00
HE21 A:GLN213 2.4 53.7 1.0
H A:LYS212 2.5 62.2 1.0
HB2 A:LYS212 2.6 70.5 1.0
HD2 A:PRO211 2.8 57.8 1.0
HA A:PHE210 2.8 59.6 1.0
HG2 A:GLN213 2.9 51.4 1.0
NE2 A:GLN213 3.2 44.7 1.0
N A:LYS212 3.4 51.8 1.0
C A:PHE210 3.5 49.9 1.0
CA A:PHE210 3.5 49.6 1.0
CB A:LYS212 3.5 58.8 1.0
CD A:PRO211 3.6 48.2 1.0
N A:PRO211 3.7 48.7 1.0
HB3 A:PHE210 3.7 56.6 1.0
HD1 A:PHE210 3.7 54.5 1.0
CG A:GLN213 3.8 42.8 1.0
H A:GLN213 3.8 57.2 1.0
HE22 A:GLN213 3.8 53.7 1.0
HD2 A:LYS212 3.9 83.3 1.0
CA A:LYS212 3.9 54.9 1.0
HG2 A:PRO211 3.9 58.4 1.0
CD A:GLN213 4.0 43.6 1.0
O A:PHE210 4.0 51.0 1.0
N A:GLN213 4.1 47.7 1.0
CB A:PHE210 4.1 47.1 1.0
HB3 A:LYS212 4.1 70.5 1.0
HG3 A:GLN213 4.2 51.4 1.0
HD11 A:LEU274 4.2 61.0 1.0
HG3 A:LYS212 4.2 77.2 1.0
HD13 A:LEU274 4.2 61.0 1.0
HD3 A:PRO211 4.3 57.8 1.0
CG A:LYS212 4.3 64.3 1.0
C A:LYS212 4.3 51.8 1.0
CG A:PRO211 4.3 48.6 1.0
C A:PRO211 4.4 50.4 1.0
CD1 A:PHE210 4.5 45.4 1.0
CD A:LYS212 4.6 69.4 1.0
O A:THR209 4.6 53.1 1.0
CA A:PRO211 4.6 48.6 1.0
CD1 A:LEU274 4.6 50.8 1.0
N A:PHE210 4.7 51.0 1.0
HA A:LYS212 4.8 65.8 1.0
CG A:PHE210 4.8 45.6 1.0
CB A:GLN213 4.8 42.4 1.0
HD12 A:LEU274 4.9 61.0 1.0
HB2 A:PHE210 4.9 56.6 1.0
HB2 A:GLN213 5.0 50.8 1.0

Reference:

M.Flecken, H.Wang, L.Popilka, F.U.Hartl, A.Bracher, M.Hayer-Hartl. Dual Role of Rca-Like Protein in Rubisco Metabolic Repair and Carboxysome Organization To Be Published.
Page generated: Mon Jul 29 17:55:13 2024

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