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Zinc in PDB 6b00: Thermostabilized Mutant of Human Carbonic Anhydrase II - A65T L100H K154N L224S L240P A248T

Enzymatic activity of Thermostabilized Mutant of Human Carbonic Anhydrase II - A65T L100H K154N L224S L240P A248T

All present enzymatic activity of Thermostabilized Mutant of Human Carbonic Anhydrase II - A65T L100H K154N L224S L240P A248T:
4.2.1.1;

Protein crystallography data

The structure of Thermostabilized Mutant of Human Carbonic Anhydrase II - A65T L100H K154N L224S L240P A248T, PDB code: 6b00 was solved by K.M.Kean, P.A.Karplus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.79 / 0.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.620, 43.760, 57.990, 90.00, 100.72, 90.00
R / Rfree (%) 12 / 14.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Thermostabilized Mutant of Human Carbonic Anhydrase II - A65T L100H K154N L224S L240P A248T (pdb code 6b00). 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 Thermostabilized Mutant of Human Carbonic Anhydrase II - A65T L100H K154N L224S L240P A248T, PDB code: 6b00:

Zinc binding site 1 out of 1 in 6b00

Go back to Zinc Binding Sites List in 6b00
Zinc binding site 1 out of 1 in the Thermostabilized Mutant of Human Carbonic Anhydrase II - A65T L100H K154N L224S L240P A248T


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thermostabilized Mutant of Human Carbonic Anhydrase II - A65T L100H K154N L224S L240P A248T within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:7.6
occ:0.20
 O A:HOH415 1.1 13.9 0.8
O A:HOH401 2.1 13.1 0.2
NE2 A:HIS94 2.1 12.9 1.0
NE2 A:HIS96 2.1 10.4 1.0
ND1 A:HIS119 2.1 8.4 1.0
CD2 A:HIS94 3.0 11.1 1.0
CD2 A:HIS96 3.0 10.7 1.0
CE1 A:HIS119 3.0 8.8 1.0
HD2 A:HIS96 3.0 12.8 1.0
HD2 A:HIS94 3.1 13.3 1.0
HE1 A:HIS119 3.1 10.5 1.0
CE1 A:HIS94 3.1 11.6 1.0
CG A:HIS119 3.2 6.8 1.0
HB2 A:HIS119 3.2 7.7 1.0
CE1 A:HIS96 3.2 9.9 1.0
H2 A:GOL301 3.3 28.0 1.0
HE1 A:HIS94 3.4 13.9 1.0
HG1 A:THR199 3.4 9.8 1.0
HE1 A:HIS96 3.5 11.9 1.0
CB A:HIS119 3.6 6.4 1.0
O1 A:GOL301 3.7 16.4 1.0
O A:HOH683 3.8 24.6 1.0
HB3 A:HIS119 3.8 7.7 1.0
OG1 A:THR199 3.8 8.1 1.0
O A:HOH429 3.8 21.5 0.8
OE1 A:GLU106 3.9 9.6 1.0
CG A:HIS94 4.1 8.2 1.0
NE2 A:HIS119 4.1 8.5 1.0
ND1 A:HIS94 4.1 10.3 1.0
C2 A:GOL301 4.2 23.3 1.0
CG A:HIS96 4.2 7.9 1.0
H12 A:GOL301 4.2 25.3 1.0
HH2 A:TRP209 4.2 12.9 1.0
ND1 A:HIS96 4.2 9.3 1.0
C1 A:GOL301 4.3 21.1 1.0
CD2 A:HIS119 4.3 7.4 1.0
HO2 A:GOL301 4.5 45.1 1.0
CD A:GLU106 4.8 7.6 1.0
O2 A:GOL301 4.8 37.6 1.0
HE2 A:HIS119 4.9 10.2 1.0
HD1 A:HIS94 4.9 12.3 1.0
O A:HOH479 5.0 36.0 1.0

Reference:

K.M.Kean, J.J.Porter, R.A.Mehl, P.A.Karplus. Structural Insights Into A Thermostable Variant of Human Carbonic Anhydrase II. Protein Sci. V. 27 573 2018.
ISSN: ESSN 1469-896X
PubMed: 29139171
DOI: 10.1002/PRO.3347
Page generated: Mon Oct 28 17:45:50 2024

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