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Calcium in PDB 1mks: Carboxylic Ester Hydrolase, Trigonal Form of the Triple Mutant

Enzymatic activity of Carboxylic Ester Hydrolase, Trigonal Form of the Triple Mutant

All present enzymatic activity of Carboxylic Ester Hydrolase, Trigonal Form of the Triple Mutant:
3.1.1.4;

Protein crystallography data

The structure of Carboxylic Ester Hydrolase, Trigonal Form of the Triple Mutant, PDB code: 1mks was solved by M.Sundaralingam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.90
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 47.080, 47.080, 102.370, 90.00, 90.00, 120.00
R / Rfree (%) 18.6 / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Carboxylic Ester Hydrolase, Trigonal Form of the Triple Mutant (pdb code 1mks). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Carboxylic Ester Hydrolase, Trigonal Form of the Triple Mutant, PDB code: 1mks:

Calcium binding site 1 out of 1 in 1mks

Go back to Calcium Binding Sites List in 1mks
Calcium binding site 1 out of 1 in the Carboxylic Ester Hydrolase, Trigonal Form of the Triple Mutant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Carboxylic Ester Hydrolase, Trigonal Form of the Triple Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca124

b:25.0
occ:1.00
O A:GLY32 2.0 28.5 1.0
O A:GLY30 2.0 22.8 1.0
O A:TYR28 2.1 20.9 1.0
OD1 A:ASP49 2.7 18.3 1.0
O A:HOH201 2.8 39.0 1.0
O A:HOH202 2.8 33.1 1.0
OD2 A:ASP49 2.8 27.0 1.0
CG A:ASP49 3.1 17.4 1.0
C A:GLY32 3.2 28.3 1.0
C A:GLY30 3.2 17.9 1.0
C A:TYR28 3.3 14.0 1.0
N A:GLY30 3.6 13.3 1.0
N A:GLY32 3.8 28.5 1.0
CA A:GLY30 4.0 15.2 1.0
CA A:TYR28 4.1 14.3 1.0
CA A:GLY32 4.1 29.0 1.0
O A:HOH205 4.2 26.3 1.0
N A:GLY33 4.2 28.0 1.0
C A:LEU31 4.2 28.0 1.0
N A:LEU31 4.3 21.6 1.0
N A:CYS29 4.3 15.5 1.0
C A:CYS29 4.5 12.8 1.0
CA A:GLY33 4.5 30.0 1.0
CA A:CYS29 4.5 13.8 1.0
CB A:ASP49 4.6 15.2 1.0
CA A:LEU31 4.6 27.9 1.0
O A:HOH238 4.7 28.5 1.0
O A:CYS45 4.7 12.8 1.0
CB A:TYR28 4.7 10.4 1.0
O A:LEU31 4.8 31.7 1.0

Reference:

K.Sekar, B.Z.Yu, J.Rogers, J.Lutton, X.Liu, X.Chen, M.D.Tsai, M.K.Jain, M.Sundaralingam. Phospholipase A2 Engineering. Structural and Functional Roles of the Highly Conserved Active Site Residue Aspartate-99. Biochemistry V. 36 3104 1997.
ISSN: ISSN 0006-2960
PubMed: 9115986
DOI: 10.1021/BI961576X
Page generated: Sat Dec 12 03:07:03 2020

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