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Zinc in PDB 4ay8: Semet-Derivative of A Methyltransferase From M. Mazei

Enzymatic activity of Semet-Derivative of A Methyltransferase From M. Mazei

All present enzymatic activity of Semet-Derivative of A Methyltransferase From M. Mazei:
2.1.1.247;

Protein crystallography data

The structure of Semet-Derivative of A Methyltransferase From M. Mazei, PDB code: 4ay8 was solved by A.Hoeppner, F.Thomas, A.Rueppel, R.Hensel, W.Blankenfeldt, P.Bayer, A.Faust, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.03 / 2.10
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 125.210, 125.210, 38.880, 90.00, 90.00, 120.00
R / Rfree (%) 14.604 / 17.659

Zinc Binding Sites:

The binding sites of Zinc atom in the Semet-Derivative of A Methyltransferase From M. Mazei (pdb code 4ay8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Semet-Derivative of A Methyltransferase From M. Mazei, PDB code: 4ay8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4ay8

Go back to Zinc Binding Sites List in 4ay8
Zinc binding site 1 out of 2 in the Semet-Derivative of A Methyltransferase From M. Mazei


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Semet-Derivative of A Methyltransferase From M. Mazei within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn600

b:17.0
occ:1.00
NE2 A:HIS240 2.2 8.9 1.0
S1 A:COM500 2.4 13.2 1.0
SG A:CYS319 2.4 7.2 1.0
SG A:CYS242 2.4 12.0 1.0
C1 A:COM500 3.0 14.7 1.0
CD2 A:HIS240 3.0 9.0 1.0
CB A:CYS242 3.2 10.2 1.0
CE1 A:HIS240 3.2 7.1 1.0
CB A:CYS319 3.7 5.6 1.0
CA A:CYS319 4.2 5.1 1.0
CG A:HIS240 4.2 6.4 1.0
CA A:CYS242 4.3 9.1 1.0
ND1 A:HIS240 4.3 6.7 1.0
N A:CYS242 4.3 7.9 1.0
C2 A:COM500 4.5 15.3 1.0
N A:GLY320 4.7 5.0 1.0
O A:GLY318 5.0 5.1 1.0
C A:CYS319 5.0 4.9 1.0

Zinc binding site 2 out of 2 in 4ay8

Go back to Zinc Binding Sites List in 4ay8
Zinc binding site 2 out of 2 in the Semet-Derivative of A Methyltransferase From M. Mazei


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Semet-Derivative of A Methyltransferase From M. Mazei within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn600

b:16.6
occ:1.00
NE2 B:HIS240 2.2 7.1 1.0
S1 B:COM500 2.4 13.3 1.0
SG B:CYS319 2.4 8.0 1.0
SG B:CYS242 2.4 10.9 1.0
C1 B:COM500 3.0 15.2 1.0
CD2 B:HIS240 3.0 7.1 1.0
CB B:CYS242 3.2 9.1 1.0
CE1 B:HIS240 3.3 6.2 1.0
CB B:CYS319 3.7 4.8 1.0
CA B:CYS319 4.2 4.8 1.0
CG B:HIS240 4.2 5.0 1.0
CA B:CYS242 4.3 8.4 1.0
N B:CYS242 4.3 7.2 1.0
ND1 B:HIS240 4.3 5.2 1.0
C2 B:COM500 4.4 15.9 1.0
N B:GLY320 4.7 4.8 1.0
O B:GLY318 5.0 4.2 1.0
C B:CYS319 5.0 4.5 1.0

Reference:

A.Hoeppner, F.Thomas, A.Rueppel, R.Hensel, W.Blankenfeldt, P.Bayer, A.Faust. Structure of the Corrinoid:Coenzyme M Methyltransferase Mtaa From Methanosarcina Mazei Acta Crystallogr.,Sect.D V. 68 1549 2012.
ISSN: ISSN 0907-4449
PubMed: 23090404
DOI: 10.1107/S090744491203853X
Page generated: Wed Dec 16 05:04:17 2020

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