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Zinc 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
Iron (Fe) 8 atoms
Calcium (Ca) 12 atoms
Chlorine (Cl) 3 atoms

Zinc Binding Sites:

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

Zinc binding site 1 out of 2 in 5c2v

Go back to Zinc Binding Sites List in 5c2v
Zinc binding site 1 out of 2 in the Kuenenia Stuttgartiensis Hydrazine Synthase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Kuenenia Stuttgartiensis Hydrazine Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn904

b:46.4
occ:1.00
NE2 A:HIS587 2.0 43.7 1.0
O A:HOH1078 2.1 51.9 1.0
O2A A:HEC905 2.2 43.1 1.0
SG A:CYS303 2.3 41.0 1.0
CGA A:HEC905 2.9 34.1 1.0
CD2 A:HIS587 3.0 39.1 1.0
CE1 A:HIS587 3.0 46.8 1.0
O1A A:HEC905 3.1 44.4 1.0
CB A:CYS303 3.5 44.1 1.0
CA A:CYS303 3.9 33.8 1.0
O A:HOH1108 3.9 37.9 1.0
O A:HOH1122 4.0 43.8 1.0
CAD A:HEC905 4.1 47.8 1.0
ND1 A:HIS587 4.1 40.2 1.0
CG A:HIS587 4.1 41.8 1.0
CBA A:HEC905 4.3 36.1 1.0
O2D A:HEC905 4.4 45.6 1.0
O A:ASN302 4.4 44.5 1.0
ND2 A:ASN302 4.4 32.4 1.0
N A:CYS303 4.4 39.5 1.0
C A:ASN302 4.6 29.5 1.0
CHA A:HEC905 4.8 50.8 1.0
C3D A:HEC905 4.8 36.7 1.0

Zinc binding site 2 out of 2 in 5c2v

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Kuenenia Stuttgartiensis Hydrazine Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn904

b:53.3
occ:1.00
NE2 D:HIS587 2.1 49.6 1.0
O2A D:HEC905 2.1 67.0 1.0
O D:HOH1047 2.1 63.8 1.0
SG D:CYS303 2.3 37.0 1.0
CGA D:HEC905 2.9 59.0 1.0
CD2 D:HIS587 3.0 39.7 1.0
CE1 D:HIS587 3.0 49.9 1.0
O1A D:HEC905 3.2 62.2 1.0
CB D:CYS303 3.6 61.1 1.0
CAD D:HEC905 4.0 55.1 1.0
O D:HOH1042 4.0 60.8 1.0
CA D:CYS303 4.1 51.3 1.0
ND1 D:HIS587 4.1 48.0 1.0
ND2 D:ASN302 4.1 32.0 1.0
CG D:HIS587 4.1 42.3 1.0
O D:ASN302 4.2 43.3 1.0
CBA D:HEC905 4.3 45.4 1.0
CHA D:HEC905 4.4 67.9 1.0
O2D D:HEC905 4.5 42.5 1.0
C D:ASN302 4.6 46.1 1.0
C3D D:HEC905 4.6 60.0 1.0
N D:CYS303 4.6 43.8 1.0
C4D D:HEC905 4.8 56.0 1.0
CAA D:HEC905 5.0 41.9 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: Wed Dec 16 06:05:51 2020

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