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Chlorine in PDB 5c2v: Kuenenia Stuttgartiensis Hydrazine Synthase

Protein crystallography data

The structure of Kuenenia Stuttgartiensis Hydrazine Synthase, PDB code: 5c2v was solved by A.Dietl, C.Ferousi, W.J.Maalcke, A.Menzel, S.De Vries, J.T.Keltjens, M.S.M.Jetten, B.Kartal, T.R.M.Barends, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.70
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 464.540, 464.540, 145.750, 90.00, 90.00, 120.00
R / Rfree (%) 23.5 / 27.1

Other elements in 5c2v:

The structure of Kuenenia Stuttgartiensis Hydrazine Synthase also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Zinc (Zn) 2 atoms
Iron (Fe) 8 atoms
Calcium (Ca) 12 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Kuenenia Stuttgartiensis Hydrazine Synthase (pdb code 5c2v). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Kuenenia Stuttgartiensis Hydrazine Synthase, PDB code: 5c2v:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 5c2v

Go back to Chlorine Binding Sites List in 5c2v
Chlorine binding site 1 out of 3 in the Kuenenia Stuttgartiensis Hydrazine Synthase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Kuenenia Stuttgartiensis Hydrazine Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl901

b:14.9
occ:0.50
 CL A:CL901 0.0 14.9 0.5
OG A:SER590 2.6 52.1 1.0
CL A:CL901 3.1 40.3 0.5
N A:GLY585 3.2 42.0 1.0
N A:TYR588 3.2 43.5 1.0
O A:GLY585 3.3 37.8 1.0
CB A:TYR588 3.3 42.9 1.0
CB A:SER590 3.4 32.0 1.0
N A:SER590 3.4 42.2 1.0
C A:GLY585 3.6 40.4 1.0
CA A:GLY585 3.7 34.9 1.0
CA A:TYR588 3.7 26.0 1.0
N A:GLY589 3.7 26.4 1.0
CE2 A:TYR591 3.7 39.8 1.0
CA A:SER590 3.9 42.8 1.0
N A:SER584 4.0 40.7 1.0
CD2 A:TYR591 4.0 34.8 1.0
C A:TYR588 4.0 28.2 1.0
CB A:SER584 4.1 26.0 1.0
C A:SER584 4.1 35.5 1.0
CD2 A:TYR588 4.2 26.0 1.0
CG A:TYR588 4.3 43.4 1.0
CA A:SER584 4.3 30.8 1.0
C A:HIS587 4.3 39.7 1.0
N A:TYR591 4.4 38.5 1.0
C A:GLY589 4.4 44.0 1.0
N A:HIS587 4.5 34.2 1.0
N A:CYS586 4.5 49.8 1.0
CZ A:TYR591 4.5 45.1 1.0
CA A:GLY589 4.6 33.2 1.0
CB A:CYS583 4.6 22.8 1.0
CA A:HIS587 4.6 41.5 1.0
C A:SER590 4.7 43.0 1.0
C A:CYS583 4.7 43.7 1.0
OH A:TYR591 4.9 30.0 1.0
CG A:TYR591 4.9 39.7 1.0
C A:CYS586 4.9 34.5 1.0

Chlorine binding site 2 out of 3 in 5c2v

Go back to Chlorine Binding Sites List in 5c2v
Chlorine binding site 2 out of 3 in the Kuenenia Stuttgartiensis Hydrazine Synthase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Kuenenia Stuttgartiensis Hydrazine Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl901

b:40.3
occ:0.50
 CL A:CL901 0.0 40.3 0.5
N A:GLY589 2.7 26.4 1.0
CL A:CL901 3.1 14.9 0.5
N A:SER590 3.1 42.2 1.0
CA A:GLY589 3.2 33.2 1.0
CZ A:TYR591 3.2 45.1 1.0
CE1 A:TYR591 3.2 36.7 1.0
CE2 A:TYR591 3.2 39.8 1.0
CD1 A:TYR591 3.2 38.6 1.0
CD2 A:TYR591 3.2 34.8 1.0
N A:TYR591 3.3 38.5 1.0
CG A:TYR591 3.3 39.7 1.0
C A:GLY589 3.3 44.0 1.0
O A:HOH1108 3.4 37.9 1.0
N A:TYR588 3.4 43.5 1.0
C A:HIS587 3.8 39.7 1.0
C A:TYR588 3.8 28.2 1.0
CA A:HIS587 3.9 41.5 1.0
OH A:TYR591 4.0 30.0 1.0
N A:ARG592 4.0 45.2 1.0
OG A:SER590 4.0 52.1 1.0
CA A:TYR591 4.1 27.7 1.0
CA A:SER590 4.1 42.8 1.0
C A:SER590 4.2 43.0 1.0
CA A:TYR588 4.2 26.0 1.0
CB A:TYR591 4.2 26.2 1.0
O A:GLY589 4.2 40.0 1.0
C A:TYR591 4.3 39.1 1.0
CB A:ARG592 4.5 52.3 1.0
O A:HIS587 4.6 39.2 1.0
CB A:SER590 4.6 32.0 1.0
N A:HIS587 4.6 34.2 1.0
O A:TYR588 4.9 46.5 1.0
CB A:TYR588 4.9 42.9 1.0
CA A:ARG592 4.9 35.2 1.0

Chlorine binding site 3 out of 3 in 5c2v

Go back to Chlorine Binding Sites List in 5c2v
Chlorine binding site 3 out of 3 in the Kuenenia Stuttgartiensis Hydrazine Synthase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Kuenenia Stuttgartiensis Hydrazine Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl901

b:60.7
occ:1.00
 OG D:SER590 2.8 58.6 1.0
N D:GLY585 3.2 52.5 1.0
O D:GLY585 3.3 54.5 1.0
N D:TYR588 3.3 53.9 1.0
CB D:SER590 3.4 57.0 1.0
N D:SER590 3.4 59.3 1.0
CB D:TYR588 3.5 47.1 1.0
CE2 D:TYR591 3.6 60.0 1.0
C D:GLY585 3.6 68.4 1.0
N D:GLY589 3.6 50.5 1.0
CA D:TYR588 3.8 41.2 1.0
CA D:GLY585 3.8 68.6 1.0
CD2 D:TYR591 3.9 49.0 1.0
N D:SER584 3.9 34.4 1.0
CA D:SER590 4.0 57.5 1.0
C D:TYR588 4.1 38.2 1.0
CB D:SER584 4.1 34.0 1.0
C D:SER584 4.2 55.4 1.0
CA D:SER584 4.3 43.0 1.0
CD2 D:TYR588 4.3 57.2 1.0
C D:HIS587 4.3 58.4 1.0
CZ D:TYR591 4.3 64.1 1.0
CG D:TYR588 4.4 60.3 1.0
N D:HIS587 4.4 52.3 1.0
N D:TYR591 4.4 50.4 1.0
C D:GLY589 4.4 63.3 1.0
CB D:CYS583 4.5 39.5 1.0
N D:CYS586 4.5 70.9 1.0
CA D:GLY589 4.6 44.8 1.0
CA D:HIS587 4.6 47.6 1.0
C D:CYS583 4.7 47.0 1.0
C D:SER590 4.7 55.3 1.0
OH D:TYR591 4.7 45.2 1.0
CG D:TYR591 4.8 61.3 1.0
C D:CYS586 4.9 51.4 1.0
CA D:CYS583 5.0 46.1 1.0
OG D:SER584 5.0 65.7 1.0

Reference:

A.Dietl, C.Ferousi, W.J.Maalcke, A.Menzel, S.De Vries, J.T.Keltjens, M.S.Jetten, B.Kartal, T.R.Barends. The Inner Workings of the Hydrazine Synthase Multiprotein Complex. Nature V. 527 394 2015.
ISSN: ESSN 1476-4687
PubMed: 26479033
DOI: 10.1038/NATURE15517
Page generated: Sat Jul 12 00:39:35 2025

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