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Zinc in PDB 6lvw: Polyextremophilic Beta-Galactosidase From the Antarctic Haloarchaeon Halorubrum Lacusprofundi

Enzymatic activity of Polyextremophilic Beta-Galactosidase From the Antarctic Haloarchaeon Halorubrum Lacusprofundi

All present enzymatic activity of Polyextremophilic Beta-Galactosidase From the Antarctic Haloarchaeon Halorubrum Lacusprofundi:
3.2.1.23;

Protein crystallography data

The structure of Polyextremophilic Beta-Galactosidase From the Antarctic Haloarchaeon Halorubrum Lacusprofundi, PDB code: 6lvw was solved by R.Muhammad, S.T.Arold, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.36 / 2.49
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 100.130, 100.130, 137.430, 90.00, 90.00, 120.00
R / Rfree (%) 24.6 / 30.8

Other elements in 6lvw:

The structure of Polyextremophilic Beta-Galactosidase From the Antarctic Haloarchaeon Halorubrum Lacusprofundi also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Polyextremophilic Beta-Galactosidase From the Antarctic Haloarchaeon Halorubrum Lacusprofundi (pdb code 6lvw). 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 Polyextremophilic Beta-Galactosidase From the Antarctic Haloarchaeon Halorubrum Lacusprofundi, PDB code: 6lvw:

Zinc binding site 1 out of 1 in 6lvw

Go back to Zinc Binding Sites List in 6lvw
Zinc binding site 1 out of 1 in the Polyextremophilic Beta-Galactosidase From the Antarctic Haloarchaeon Halorubrum Lacusprofundi


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Polyextremophilic Beta-Galactosidase From the Antarctic Haloarchaeon Halorubrum Lacusprofundi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn801

b:0.9
occ:1.00
 SG A:CYS156 2.4 76.3 1.0
SG A:CYS151 2.7 0.9 1.0
CB A:CYS151 2.8 68.4 1.0
SG A:CYS107 2.8 0.2 1.0
SG A:CYS153 2.9 77.8 1.0
CB A:CYS153 3.0 64.8 1.0
CB A:CYS107 3.5 80.4 1.0
N A:CYS153 3.5 66.2 1.0
CA A:CYS153 3.9 66.0 1.0
CA A:GLN90 3.9 69.3 1.0
CA A:CYS151 4.0 64.2 1.0
C A:CYS151 4.0 71.9 1.0
CG A:GLN90 4.1 59.6 1.0
CB A:CYS156 4.1 63.9 1.0
N A:GLU91 4.2 58.8 1.0
N A:TYR152 4.2 79.2 1.0
CB A:GLN90 4.3 71.0 1.0
O A:CYS151 4.5 83.6 1.0
O A:ARG89 4.5 51.1 1.0
C A:GLN90 4.6 62.2 1.0
CA A:CYS107 4.6 73.6 1.0
N A:CYS156 4.6 69.5 1.0
C A:TYR152 4.7 75.8 1.0
C A:CYS153 4.7 73.9 1.0
N A:GLN90 5.0 72.9 1.0
N A:CYS151 5.0 62.1 1.0

Reference:

R.Karan, S.Mathew, R.Muhammad, D.B.Bautista, M.Vogler, J.Eppinger, R.Oliva, L.Cavallo, S.T.Arold, M.Rueping. Understanding High-Salt and Cold Adaptation of A Polyextremophilic Enzyme. Microorganisms V. 8 2020.
ISSN: ISSN 2076-2607
PubMed: 33081237
DOI: 10.3390/MICROORGANISMS8101594
Page generated: Tue Oct 29 02:50:17 2024

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