Zinc in PDB 7aru: L254N Mutant of Carboxypeptidase T From Thermoactinomyces Vulgaris N- Sulfamoyl-L-Valine

Enzymatic activity of L254N Mutant of Carboxypeptidase T From Thermoactinomyces Vulgaris N- Sulfamoyl-L-Valine

All present enzymatic activity of L254N Mutant of Carboxypeptidase T From Thermoactinomyces Vulgaris N- Sulfamoyl-L-Valine:
3.4.17.18;

Protein crystallography data

The structure of L254N Mutant of Carboxypeptidase T From Thermoactinomyces Vulgaris N- Sulfamoyl-L-Valine, PDB code: 7aru was solved by V.I.Timofeev, V.K.Akparov, I.P.Kuranova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.91 / 2.05
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 158.110, 158.110, 104.042, 90.00, 90.00, 120.00
R / Rfree (%) 15.3 / 16.8

Other elements in 7aru:

The structure of L254N Mutant of Carboxypeptidase T From Thermoactinomyces Vulgaris N- Sulfamoyl-L-Valine also contains other interesting chemical elements:

Calcium (Ca) 5 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the L254N Mutant of Carboxypeptidase T From Thermoactinomyces Vulgaris N- Sulfamoyl-L-Valine (pdb code 7aru). 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 L254N Mutant of Carboxypeptidase T From Thermoactinomyces Vulgaris N- Sulfamoyl-L-Valine, PDB code: 7aru:

Zinc binding site 1 out of 1 in 7aru

Go back to Zinc Binding Sites List in 7aru
Zinc binding site 1 out of 1 in the L254N Mutant of Carboxypeptidase T From Thermoactinomyces Vulgaris N- Sulfamoyl-L-Valine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of L254N Mutant of Carboxypeptidase T From Thermoactinomyces Vulgaris N- Sulfamoyl-L-Valine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:11.0
occ:1.00
 ND1 A:HIS69 2.0 10.1 1.0
ND1 A:HIS204 2.1 9.3 1.0
N19 A:NO5402 2.1 18.5 1.0
OE1 A:GLU72 2.2 10.3 1.0
OE2 A:GLU72 2.2 10.3 1.0
CD A:GLU72 2.5 10.2 1.0
O21 A:NO5402 2.8 18.8 1.0
CE1 A:HIS69 2.9 10.3 1.0
CE1 A:HIS204 3.0 9.5 1.0
S18 A:NO5402 3.0 22.0 1.0
CG A:HIS204 3.1 9.6 1.0
CG A:HIS69 3.1 10.3 1.0
CB A:HIS204 3.4 9.7 1.0
CB A:HIS69 3.5 10.2 1.0
O A:THR205 3.9 10.3 1.0
O A:HOH661 4.0 12.8 1.0
CG A:GLU72 4.0 10.1 1.0
O20 A:NO5402 4.1 19.0 1.0
N17 A:NO5402 4.1 21.7 1.0
NE2 A:HIS69 4.1 10.2 1.0
O A:HOH518 4.1 19.3 1.0
NE2 A:HIS204 4.2 9.3 1.0
CD2 A:HIS69 4.2 10.3 1.0
CD2 A:HIS204 4.2 9.3 1.0
C13 A:NO5402 4.2 21.4 1.0
CA A:HIS204 4.3 9.9 1.0
N A:THR205 4.5 10.5 1.0
NH1 A:ARG129 4.6 12.5 1.0
O15 A:NO5402 4.6 16.5 1.0
OE2 A:GLU277 4.6 15.9 1.0
C14 A:NO5402 4.6 18.8 1.0
OE1 A:GLU277 4.8 13.8 1.0
CA A:HIS69 4.8 10.3 1.0
N A:HIS69 4.9 10.3 1.0
CB A:GLU72 4.9 10.4 1.0
C A:HIS204 5.0 10.2 1.0
C A:THR205 5.0 10.7 1.0

Reference:

V.I.Timofeev, V.K.Akparov, I.P.Kuranova. L254N Mutant of Carboxypeptidase T From Thermoactinomyces Vulgaris N-Sulfamoyl-L-Valine To Be Published.
Page generated: Wed Dec 16 13:35:38 2020

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