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Calcium in PDB 1el1: X-Ray Crystal Structure Analysis of Canine Milk Lysozyme (Holo-Type)

Enzymatic activity of X-Ray Crystal Structure Analysis of Canine Milk Lysozyme (Holo-Type)

All present enzymatic activity of X-Ray Crystal Structure Analysis of Canine Milk Lysozyme (Holo-Type):
3.2.1.17;

Protein crystallography data

The structure of X-Ray Crystal Structure Analysis of Canine Milk Lysozyme (Holo-Type), PDB code: 1el1 was solved by T.Koshiba, M.Yao, I.Tanaka, K.Nitta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.90
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 31.300, 31.300, 202.500, 90.00, 90.00, 120.00
R / Rfree (%) 15.9 / 25.7

Calcium Binding Sites:

The binding sites of Calcium atom in the X-Ray Crystal Structure Analysis of Canine Milk Lysozyme (Holo-Type) (pdb code 1el1). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the X-Ray Crystal Structure Analysis of Canine Milk Lysozyme (Holo-Type), PDB code: 1el1:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1el1

Go back to Calcium Binding Sites List in 1el1
Calcium binding site 1 out of 2 in the X-Ray Crystal Structure Analysis of Canine Milk Lysozyme (Holo-Type)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of X-Ray Crystal Structure Analysis of Canine Milk Lysozyme (Holo-Type) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca130

b:31.4
occ:1.00
O A:ASN87 2.3 28.0 1.0
O A:LYS82 2.3 27.2 1.0
OD1 A:ASP85 2.5 33.2 1.0
OD1 A:ASP91 2.5 23.0 1.0
OD1 A:ASP90 2.6 32.5 1.0
O A:HOH133 2.7 21.1 1.0
O A:HOH202 2.7 30.7 1.0
CG A:ASP90 3.1 28.6 1.0
OD2 A:ASP90 3.3 26.1 1.0
CG A:ASP85 3.4 31.5 1.0
CG A:ASP91 3.6 22.9 1.0
C A:ASN87 3.6 29.3 1.0
OD2 A:ASP85 3.7 30.8 1.0
C A:LYS82 3.7 27.3 1.0
OD2 A:ASP91 3.9 21.5 1.0
CA A:ILE88 4.2 26.5 1.0
N A:ASP90 4.2 27.2 1.0
CA A:PHE83 4.3 28.0 1.0
N A:ILE88 4.4 27.3 1.0
N A:PHE83 4.4 27.7 1.0
N A:ASP91 4.4 24.4 1.0
CB A:ASP90 4.4 28.1 1.0
N A:ASN87 4.5 30.6 1.0
CA A:ASN87 4.6 29.8 1.0
CA A:ASP90 4.6 26.9 1.0
C A:ASP90 4.7 25.7 1.0
C A:ILE88 4.7 26.6 1.0
O A:ASP85 4.7 27.8 1.0
CA A:LYS82 4.7 25.9 1.0
N A:ASP89 4.8 26.3 1.0
CD1 A:PHE83 4.8 30.6 1.0
CB A:ASP85 4.8 29.1 1.0
C A:PHE83 4.8 27.9 1.0
CB A:LYS82 4.8 26.7 1.0
C A:ASP85 4.8 29.8 1.0
CB A:ASP91 4.9 23.7 1.0
CB A:ASN87 4.9 30.8 1.0
N A:ASP85 4.9 28.6 1.0

Calcium binding site 2 out of 2 in 1el1

Go back to Calcium Binding Sites List in 1el1
Calcium binding site 2 out of 2 in the X-Ray Crystal Structure Analysis of Canine Milk Lysozyme (Holo-Type)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of X-Ray Crystal Structure Analysis of Canine Milk Lysozyme (Holo-Type) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca130

b:30.7
occ:1.00
O B:ASN87 2.3 30.8 1.0
O B:LYS82 2.4 28.4 1.0
OD1 B:ASP85 2.6 31.3 1.0
OD1 B:ASP90 2.6 25.6 1.0
OD1 B:ASP91 2.6 28.5 1.0
O B:HOH144 2.7 28.8 1.0
O B:HOH185 2.8 57.3 1.0
C B:ASN87 3.5 30.3 1.0
CG B:ASP91 3.5 27.1 1.0
C B:LYS82 3.6 28.8 1.0
CG B:ASP90 3.6 26.7 1.0
CG B:ASP85 3.7 32.0 1.0
CA B:ILE88 3.8 28.4 1.0
CA B:PHE83 3.9 27.9 1.0
N B:ILE88 4.0 29.2 1.0
OD2 B:ASP90 4.0 27.4 1.0
OD2 B:ASP85 4.1 33.5 1.0
OD2 B:ASP91 4.1 27.4 1.0
N B:PHE83 4.2 28.4 1.0
C B:PHE83 4.4 27.2 1.0
C B:ILE88 4.4 27.2 1.0
CB B:ASP91 4.4 25.5 1.0
N B:ASP91 4.4 25.2 1.0
CA B:ASN87 4.5 30.1 1.0
N B:ASN87 4.5 30.7 1.0
CD1 B:PHE83 4.5 29.3 1.0
N B:ASP85 4.6 30.0 1.0
N B:ASP90 4.7 27.4 1.0
N B:LEU84 4.7 26.9 1.0
N B:ASP89 4.8 27.5 1.0
CA B:LYS82 4.8 28.4 1.0
O B:ASP85 4.9 29.6 1.0
O B:PHE83 4.9 26.0 1.0
CB B:ASN87 4.9 30.2 1.0
CA B:ASP91 4.9 25.4 1.0
CB B:ASP85 4.9 31.1 1.0
CB B:ASP90 4.9 27.1 1.0
C B:ASP85 5.0 31.5 1.0
O B:ILE88 5.0 26.6 1.0
CB B:ILE88 5.0 26.9 1.0
C B:ASP90 5.0 26.6 1.0

Reference:

T.Koshiba, M.Yao, I.Tanaka, K.Nitta. Calcium Induced Conformational Changes of Canine Milk Lysozyme Revealed By Structural and Thermodynamical Evidences To Be Published.
Page generated: Sat Dec 12 02:54:17 2020

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