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Zinc in PDB 2wyh: Structure of the Streptococcus Pyogenes Family GH38 Alpha- Mannosidase

Enzymatic activity of Structure of the Streptococcus Pyogenes Family GH38 Alpha- Mannosidase

All present enzymatic activity of Structure of the Streptococcus Pyogenes Family GH38 Alpha- Mannosidase:
3.2.1.24;

Protein crystallography data

The structure of Structure of the Streptococcus Pyogenes Family GH38 Alpha- Mannosidase, PDB code: 2wyh was solved by M.D.L.Suits, Y.Zhu, E.J.Taylor, D.L.Zechel, H.J.Gilbert, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 127.00 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 92.573, 88.502, 134.688, 90.00, 108.97, 90.00
R / Rfree (%) 17.7 / 20.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Streptococcus Pyogenes Family GH38 Alpha- Mannosidase (pdb code 2wyh). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of the Streptococcus Pyogenes Family GH38 Alpha- Mannosidase, PDB code: 2wyh:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2wyh

Go back to Zinc Binding Sites List in 2wyh
Zinc binding site 1 out of 2 in the Structure of the Streptococcus Pyogenes Family GH38 Alpha- Mannosidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Streptococcus Pyogenes Family GH38 Alpha- Mannosidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn902

b:29.8
occ:1.00
NE2 A:HIS351 2.2 20.6 1.0
NE2 A:HIS13 2.3 12.7 1.0
OD1 A:ASP15 2.4 18.9 1.0
OD2 A:ASP125 2.5 24.6 1.0
O A:HOH2010 2.7 26.9 1.0
CE1 A:HIS351 3.1 22.2 1.0
CD2 A:HIS13 3.1 13.1 1.0
CD2 A:HIS351 3.3 19.3 1.0
CG A:ASP15 3.3 18.4 1.0
CE1 A:HIS13 3.3 13.1 1.0
CG A:ASP125 3.4 21.7 1.0
CB A:ASP125 3.4 18.4 1.0
OD2 A:ASP15 3.6 22.7 1.0
O A:HOH2036 4.2 18.5 1.0
OD2 A:ASP352 4.2 17.8 1.0
ND1 A:HIS351 4.2 20.4 1.0
CG A:HIS13 4.3 13.0 1.0
CG A:HIS351 4.4 18.0 1.0
ND1 A:HIS13 4.4 12.6 1.0
OD1 A:ASP125 4.6 25.0 1.0
OH A:TYR192 4.6 20.6 1.0
CB A:ASP15 4.7 15.9 1.0
O A:HOH2077 4.8 13.1 1.0
CA A:ASP125 4.9 17.2 1.0
OD1 A:ASP352 4.9 14.9 1.0
CG A:ASP352 4.9 15.2 1.0
O A:HOH2216 5.0 14.6 1.0

Zinc binding site 2 out of 2 in 2wyh

Go back to Zinc Binding Sites List in 2wyh
Zinc binding site 2 out of 2 in the Structure of the Streptococcus Pyogenes Family GH38 Alpha- Mannosidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Streptococcus Pyogenes Family GH38 Alpha- Mannosidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn902

b:28.4
occ:1.00
NE2 B:HIS351 2.2 17.0 1.0
OD1 B:ASP15 2.2 20.1 1.0
NE2 B:HIS13 2.2 12.7 1.0
OD2 B:ASP125 2.4 21.0 1.0
CE1 B:HIS351 2.9 19.5 1.0
CD2 B:HIS13 3.1 12.1 1.0
O B:HOH2192 3.1 29.3 1.0
CG B:ASP15 3.1 17.5 1.0
CG B:ASP125 3.2 18.9 1.0
CE1 B:HIS13 3.3 13.9 1.0
CB B:ASP125 3.3 15.7 1.0
CD2 B:HIS351 3.4 17.4 1.0
OD2 B:ASP15 3.4 22.2 1.0
ND1 B:HIS351 4.1 19.4 1.0
OD2 B:ASP352 4.2 16.8 1.0
O B:HOH2031 4.2 18.1 1.0
CG B:HIS13 4.3 12.2 1.0
ND1 B:HIS13 4.3 14.0 1.0
CG B:HIS351 4.4 14.8 1.0
OD1 B:ASP125 4.4 21.5 1.0
CB B:ASP15 4.5 14.4 1.0
OH B:TYR192 4.6 15.8 1.0
CA B:ASP125 4.9 15.0 1.0
CG B:ASP352 4.9 14.4 1.0
O B:HOH2078 4.9 16.0 1.0
OD1 B:ASP352 4.9 12.8 1.0
O B:HOH2193 4.9 10.4 1.0

Reference:

M.D.L.Suits, Y.Zhu, E.J.Taylor, D.L.Zechel, H.J.Gilbert, G.J.Davies. Structure and Kinetic Investigation of Streptococcus Pyogenes Family GH38 Alpha-Mannosidase Plos One V. 5 E9006 2010.
ISSN: ESSN 1932-6203
PubMed: 20140249
DOI: 10.1371/JOURNAL.PONE.0009006
Page generated: Thu Oct 17 05:04:52 2024

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