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Zinc in PDB 4n0l: Methanopyrus Kandleri CSM3 Crystal Structure

Protein crystallography data

The structure of Methanopyrus Kandleri CSM3 Crystal Structure, PDB code: 4n0l was solved by A.Hrle, A.A.Su, J.Ebert, C.Benda, E.Conti, L.Randau, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 69.49 / 2.37
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 95.753, 101.017, 174.167, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 21.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Methanopyrus Kandleri CSM3 Crystal Structure (pdb code 4n0l). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Methanopyrus Kandleri CSM3 Crystal Structure, PDB code: 4n0l:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4n0l

Go back to Zinc Binding Sites List in 4n0l
Zinc binding site 1 out of 2 in the Methanopyrus Kandleri CSM3 Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Methanopyrus Kandleri CSM3 Crystal Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:30.6
occ:1.00
NE2 A:HIS86 2.0 26.0 1.0
SG A:CYS115 2.3 28.6 1.0
SG A:CYS118 2.3 27.5 1.0
SG A:CYS88 2.4 32.2 1.0
CD2 A:HIS86 2.8 28.9 1.0
CE1 A:HIS86 3.2 26.0 1.0
CB A:CYS115 3.2 32.6 1.0
CB A:CYS118 3.2 14.9 1.0
CB A:CYS88 3.4 20.6 1.0
N A:CYS88 3.6 27.8 1.0
N A:CYS118 3.9 21.0 1.0
CA A:CYS88 4.0 26.8 1.0
CG A:HIS86 4.0 29.7 1.0
NE1 A:TRP109 4.1 32.2 1.0
ND1 A:HIS86 4.1 28.9 1.0
CD1 A:TRP109 4.2 29.5 1.0
CA A:CYS118 4.2 20.8 1.0
O A:CYS88 4.4 26.1 1.0
C A:GLU87 4.4 28.2 1.0
C A:CYS88 4.5 29.6 1.0
CB A:VAL117 4.5 22.1 1.0
CA A:CYS115 4.6 31.1 1.0
CA A:GLU87 4.7 22.5 1.0
O A:HIS86 5.0 27.7 1.0
C A:VAL117 5.0 21.1 1.0
CG1 A:VAL117 5.0 22.2 1.0

Zinc binding site 2 out of 2 in 4n0l

Go back to Zinc Binding Sites List in 4n0l
Zinc binding site 2 out of 2 in the Methanopyrus Kandleri CSM3 Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Methanopyrus Kandleri CSM3 Crystal Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:34.5
occ:1.00
NE2 B:HIS84 2.0 29.9 1.0
SG B:CYS116 2.3 30.1 1.0
SG B:CYS86 2.3 35.1 1.0
SG B:CYS113 2.3 29.5 1.0
CD2 B:HIS84 2.9 28.0 1.0
CE1 B:HIS84 3.1 29.8 1.0
CB B:CYS113 3.2 29.5 1.0
CB B:CYS116 3.2 32.3 1.0
CB B:CYS86 3.3 31.4 1.0
N B:CYS86 3.5 37.3 1.0
NE1 B:TRP107 3.9 34.0 1.0
CA B:CYS86 3.9 33.3 1.0
N B:CYS116 4.0 33.5 1.0
CD1 B:TRP107 4.0 35.3 1.0
CG B:HIS84 4.1 29.0 1.0
ND1 B:HIS84 4.1 27.4 1.0
CA B:CYS116 4.2 32.7 1.0
O B:CYS86 4.4 37.3 1.0
C B:GLU85 4.4 38.7 1.0
C B:CYS86 4.4 35.7 1.0
CA B:CYS113 4.7 34.1 1.0
CB B:VAL115 4.7 28.5 1.0
CA B:GLU85 4.8 36.0 1.0
CE2 B:TRP107 5.0 35.2 1.0

Reference:

A.Hrle, A.A.Su, J.Ebert, C.Benda, L.Randau, E.Conti. Structure and Rna-Binding Properties of the Type III-A Crispr-Associated Protein CSM3. Rna Biol. V. 10 1670 2013.
ISSN: ISSN 1547-6286
PubMed: 24157656
DOI: 10.4161/RNA.26500
Page generated: Sun Oct 27 02:55:28 2024

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