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Zinc in PDB 1ym3: Crystal Structure of Carbonic Anhydrase RV3588C From Mycobacterium Tuberculosis

Enzymatic activity of Crystal Structure of Carbonic Anhydrase RV3588C From Mycobacterium Tuberculosis

All present enzymatic activity of Crystal Structure of Carbonic Anhydrase RV3588C From Mycobacterium Tuberculosis:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Carbonic Anhydrase RV3588C From Mycobacterium Tuberculosis, PDB code: 1ym3 was solved by A.S.Covarrubias, A.M.Larsson, M.Hogbom, J.Lindberg, T.Bergfors, C.Bjorkelid, S.L.Mowbray, T.Unge, T.A.Jones, Structural Proteomics Ineurope (Spine), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.20 / 1.75
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 56.377, 56.377, 104.192, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 22.9

Other elements in 1ym3:

The structure of Crystal Structure of Carbonic Anhydrase RV3588C From Mycobacterium Tuberculosis also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Carbonic Anhydrase RV3588C From Mycobacterium Tuberculosis (pdb code 1ym3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Carbonic Anhydrase RV3588C From Mycobacterium Tuberculosis, PDB code: 1ym3:

Zinc binding site 1 out of 1 in 1ym3

Go back to Zinc Binding Sites List in 1ym3
Zinc binding site 1 out of 1 in the Crystal Structure of Carbonic Anhydrase RV3588C From Mycobacterium Tuberculosis


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 RV3588C From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:23.3
occ:1.00
 NE2 A:HIS104 2.1 17.1 1.0
OD1 A:ASP53 2.1 20.8 1.0
SG A:CYS107 2.3 21.1 1.0
SG A:CYS51 2.4 19.9 1.0
CG A:ASP53 3.0 19.3 1.0
CE1 A:HIS104 3.0 20.1 1.0
CD2 A:HIS104 3.1 17.0 1.0
OD2 A:ASP53 3.2 23.0 1.0
CB A:CYS51 3.2 17.8 1.0
CB A:CYS107 3.3 22.1 1.0
CA A:CYS107 3.6 21.6 1.0
ND1 A:HIS104 4.1 18.8 1.0
N A:GLY108 4.2 21.5 1.0
CB A:ASP53 4.2 20.0 1.0
CG A:HIS104 4.2 18.5 1.0
C A:CYS107 4.2 20.8 1.0
O A:HOH320 4.3 27.1 1.0
C A:ASP53 4.4 20.7 1.0
N A:ASP53 4.4 18.4 1.0
N A:SER54 4.5 21.4 1.0
CA A:ASP53 4.5 19.7 1.0
N A:ALA109 4.6 21.5 1.0
CA A:CYS51 4.6 17.1 1.0
CB A:ALA109 4.8 23.2 1.0
O A:ASP53 4.8 21.4 1.0
N A:CYS107 4.8 21.4 1.0
OE2 A:GLU153 4.9 22.6 1.0
N A:GLY76 5.0 17.5 1.0
C A:CYS51 5.0 16.6 1.0

Reference:

A.Suarez Covarrubias, A.M.Larsson, M.Hogbom, J.Lindberg, T.Bergfors, C.Bjorkelid, S.L.Mowbray, T.Unge, T.A.Jones. Structure and Function of Carbonic Anhydrases From Mycobacterium Tuberculosis. J.Biol.Chem. V. 280 18782 2005.
ISSN: ISSN 0021-9258
PubMed: 15753099
DOI: 10.1074/JBC.M414348200
Page generated: Wed Oct 16 20:59:45 2024

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