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Zinc in PDB 3las: Crystal Structure of Carbonic Anhydrase From Streptococcus Mutans to 1.4 Angstrom Resolution

Enzymatic activity of Crystal Structure of Carbonic Anhydrase From Streptococcus Mutans to 1.4 Angstrom Resolution

All present enzymatic activity of Crystal Structure of Carbonic Anhydrase From Streptococcus Mutans to 1.4 Angstrom Resolution:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Carbonic Anhydrase From Streptococcus Mutans to 1.4 Angstrom Resolution, PDB code: 3las was solved by L.-L.Ma, K.-T.Wang, X.Liu, X.-D.Su, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.40
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 80.949, 80.949, 128.949, 90.00, 90.00, 120.00
R / Rfree (%) 15.4 / 18

Other elements in 3las:

The structure of Crystal Structure of Carbonic Anhydrase From Streptococcus Mutans to 1.4 Angstrom Resolution also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Carbonic Anhydrase From Streptococcus Mutans to 1.4 Angstrom Resolution (pdb code 3las). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Carbonic Anhydrase From Streptococcus Mutans to 1.4 Angstrom Resolution, PDB code: 3las:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3las

Go back to Zinc Binding Sites List in 3las
Zinc binding site 1 out of 2 in the Crystal Structure of Carbonic Anhydrase From Streptococcus Mutans to 1.4 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Carbonic Anhydrase From Streptococcus Mutans to 1.4 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn167

b:7.7
occ:1.00
NE2 A:HIS91 2.0 7.6 1.0
O A:HOH279 2.2 10.8 1.0
SG A:CYS38 2.3 7.1 1.0
SG A:CYS94 2.3 8.1 1.0
CE1 A:HIS91 3.0 7.8 1.0
CD2 A:HIS91 3.0 7.8 1.0
CB A:CYS94 3.3 7.6 1.0
CB A:CYS38 3.3 7.0 1.0
CA A:CYS94 3.5 8.0 1.0
O A:HOH303 3.5 24.1 1.0
O A:HOH325 3.6 21.0 1.0
N A:GLY95 3.8 8.5 1.0
CB A:ASP40 4.0 7.5 0.5
CB A:ASP40 4.1 7.1 0.5
O A:HOH199 4.1 7.7 1.0
ND1 A:HIS91 4.1 7.2 1.0
C A:CYS94 4.2 9.0 1.0
OD2 A:ASP40 4.2 7.0 0.5
CG A:HIS91 4.2 7.3 1.0
N A:GLY63 4.3 7.0 1.0
CA A:GLY63 4.3 7.5 1.0
CG A:ASP40 4.6 5.1 0.5
OD2 A:ASP40 4.6 13.8 0.5
CA A:CYS38 4.7 6.1 1.0
N A:ASP40 4.7 6.7 1.0
CG A:ASP40 4.7 12.1 0.5
N A:CYS94 4.8 8.8 1.0
CA A:ASP40 4.8 7.2 0.5
CA A:ASP40 4.8 6.4 0.5
CA A:GLY95 4.9 9.6 1.0
N A:ALA96 4.9 9.2 1.0

Zinc binding site 2 out of 2 in 3las

Go back to Zinc Binding Sites List in 3las
Zinc binding site 2 out of 2 in the Crystal Structure of Carbonic Anhydrase From Streptococcus Mutans to 1.4 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Carbonic Anhydrase From Streptococcus Mutans to 1.4 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn167

b:8.7
occ:1.00
NE2 B:HIS91 2.1 7.7 1.0
O B:HOH278 2.2 10.7 1.0
SG B:CYS38 2.2 8.1 1.0
SG B:CYS94 2.3 9.4 1.0
CE1 B:HIS91 3.0 8.2 1.0
CD2 B:HIS91 3.1 8.1 1.0
CB B:CYS94 3.3 9.3 1.0
CB B:CYS38 3.3 7.8 1.0
O B:HOH326 3.3 19.4 1.0
CA B:CYS94 3.6 8.7 1.0
O B:HOH307 3.7 23.9 1.0
N B:GLY95 3.8 11.2 1.0
CB B:ASP40 4.1 7.5 0.5
O B:HOH175 4.1 7.8 1.0
OD2 B:ASP40 4.1 11.1 0.5
CB B:ASP40 4.1 7.5 0.5
ND1 B:HIS91 4.1 8.4 1.0
C B:CYS94 4.2 9.9 1.0
CG B:HIS91 4.2 8.3 1.0
N B:GLY63 4.3 7.4 1.0
CA B:GLY63 4.4 8.9 1.0
OD2 B:ASP40 4.6 12.3 0.5
CG B:ASP40 4.6 8.5 0.5
CA B:CYS38 4.7 7.4 1.0
N B:ASP40 4.8 7.3 1.0
CG B:ASP40 4.8 9.4 0.5
N B:CYS94 4.8 9.3 1.0
CA B:ASP40 4.9 7.7 0.5
CA B:ASP40 4.9 7.6 0.5
CA B:GLY95 5.0 11.8 1.0

Reference:

L.-L.Ma, K.-T.Wang, X.Liu, X.-D.Su. Crystal Structure of Carbonic Anhydrase From Streptococcus Mutans to 1.4 Angstrom Resolution To Be Published.
Page generated: Sat Oct 26 08:26:58 2024

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