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Chlorine in PDB 3v3h: Kinetic and Structural Studies of Thermostabilized Mutants of Hca II.

Enzymatic activity of Kinetic and Structural Studies of Thermostabilized Mutants of Hca II.

All present enzymatic activity of Kinetic and Structural Studies of Thermostabilized Mutants of Hca II.:
4.2.1.1;

Protein crystallography data

The structure of Kinetic and Structural Studies of Thermostabilized Mutants of Hca II., PDB code: 3v3h was solved by C.D.Boone, S.Z.Fisher, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.53 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.165, 71.893, 74.576, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 22.4

Other elements in 3v3h:

The structure of Kinetic and Structural Studies of Thermostabilized Mutants of Hca II. also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Kinetic and Structural Studies of Thermostabilized Mutants of Hca II. (pdb code 3v3h). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Kinetic and Structural Studies of Thermostabilized Mutants of Hca II., PDB code: 3v3h:

Chlorine binding site 1 out of 1 in 3v3h

Go back to Chlorine Binding Sites List in 3v3h
Chlorine binding site 1 out of 1 in the Kinetic and Structural Studies of Thermostabilized Mutants of Hca II.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Kinetic and Structural Studies of Thermostabilized Mutants of Hca II. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl302

b:25.5
occ:1.00
 HE21 B:GLN158 2.4 16.8 1.0
HE3 B:LYS225 2.7 30.8 1.0
HB2 B:GLU221 2.9 31.5 1.0
O B:HOH570 3.1 31.4 1.0
NE2 B:GLN158 3.3 14.0 1.0
HG2 B:GLN222 3.3 18.0 1.0
HZ1 B:LYS225 3.3 34.0 1.0
HA B:GLN222 3.4 17.3 1.0
CE B:LYS225 3.5 25.7 1.0
HG3 B:GLN222 3.6 18.0 1.0
HG22 B:VAL161 3.6 25.1 1.0
HD2 B:LYS225 3.7 29.9 1.0
NZ B:LYS225 3.7 28.4 1.0
HZ3 B:LYS225 3.7 34.0 1.0
CB B:GLU221 3.8 26.2 1.0
HE22 B:GLN158 3.8 16.8 1.0
CG B:GLN222 3.9 15.0 1.0
N B:GLN222 3.9 21.1 1.0
C B:GLU221 3.9 21.7 1.0
OE1 B:GLN158 4.0 21.3 1.0
CA B:GLN222 4.0 14.4 1.0
CD B:GLN158 4.1 16.9 1.0
HG3 B:GLU221 4.1 49.3 1.0
H B:GLN222 4.1 25.4 1.0
CD B:LYS225 4.1 24.9 1.0
O B:GLU221 4.2 18.2 1.0
O B:HOH493 4.2 24.6 1.0
HE2 B:LYS225 4.2 30.8 1.0
CD B:GLU221 4.3 44.1 1.0
CG B:GLU221 4.3 41.1 1.0
HG B:SER219 4.3 22.0 1.0
HB3 B:GLU221 4.3 31.5 1.0
OE1 B:GLU221 4.4 51.9 1.0
HG3 B:LYS225 4.5 27.4 1.0
CG2 B:VAL161 4.5 20.9 1.0
CA B:GLU221 4.5 21.5 1.0
HZ2 B:LYS225 4.6 34.0 1.0
CB B:GLN222 4.6 18.1 1.0
HG23 B:VAL161 4.6 25.1 1.0
OE2 B:GLU221 4.6 26.1 1.0
HE22 B:GLN222 4.7 19.3 1.0
OG B:SER219 4.8 18.3 1.0
OD1 B:ASP162 4.9 22.8 1.0
HG21 B:VAL161 4.9 25.1 1.0
HD3 B:LYS225 4.9 29.9 1.0
CG B:LYS225 4.9 22.8 1.0

Reference:

Z.Fisher, C.D.Boone, S.M.Biswas, B.Venkatakrishnan, M.Aggarwal, C.Tu, M.Agbandje-Mckenna, D.Silverman, R.Mckenna. Kinetic and Structural Characterization of Thermostabilized Mutants of Human Carbonic Anhydrase II. Protein Eng.Des.Sel. V. 25 347 2012.
ISSN: ISSN 1741-0126
PubMed: 22691706
DOI: 10.1093/PROTEIN/GZS027
Page generated: Sun Jul 21 06:41:26 2024

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