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Calcium in PDB 5o8x: The X-Ray Structure of Catenated Lytic Transglycosylase SLTB1 From Pseudomonas Aeruginosa

Protein crystallography data

The structure of The X-Ray Structure of Catenated Lytic Transglycosylase SLTB1 From Pseudomonas Aeruginosa, PDB code: 5o8x was solved by T.Dominguez-Gil, R.Molina, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.26 / 2.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 115.064, 116.358, 54.865, 90.00, 118.41, 90.00
R / Rfree (%) 17.7 / 22.9

Other elements in 5o8x:

The structure of The X-Ray Structure of Catenated Lytic Transglycosylase SLTB1 From Pseudomonas Aeruginosa also contains other interesting chemical elements:

Arsenic (As) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the The X-Ray Structure of Catenated Lytic Transglycosylase SLTB1 From Pseudomonas Aeruginosa (pdb code 5o8x). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the The X-Ray Structure of Catenated Lytic Transglycosylase SLTB1 From Pseudomonas Aeruginosa, PDB code: 5o8x:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 5o8x

Go back to Calcium Binding Sites List in 5o8x
Calcium binding site 1 out of 2 in the The X-Ray Structure of Catenated Lytic Transglycosylase SLTB1 From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The X-Ray Structure of Catenated Lytic Transglycosylase SLTB1 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca401

b:81.9
occ:1.00
O A:HIS187 2.3 62.0 1.0
OD2 A:ASP196 2.4 57.3 1.0
OD1 A:ASP181 2.6 57.1 1.0
OD1 A:ASP185 2.6 69.9 1.0
OD1 A:ASP196 2.8 54.1 1.0
OD1 A:ASP183 2.8 67.0 1.0
CG A:ASP196 2.9 58.5 1.0
C A:HIS187 3.4 66.9 1.0
CG A:ASP185 3.4 72.4 1.0
CG A:ASP181 3.5 64.3 1.0
OD2 A:ASP193 3.7 60.0 1.0
CG A:ASP183 3.7 63.7 1.0
OD2 A:ASP185 3.8 77.7 1.0
OD2 A:ASP183 4.0 59.5 1.0
CA A:ASP181 4.1 54.2 1.0
N A:HIS187 4.1 68.2 1.0
CB A:ASP181 4.2 56.9 1.0
CA A:HIS187 4.2 70.7 1.0
N A:ILE188 4.2 57.4 1.0
OD2 A:ASP181 4.3 72.5 1.0
CA A:ILE188 4.3 56.0 1.0
N A:PHE182 4.3 52.4 1.0
CB A:ASP196 4.4 49.6 1.0
N A:ASP183 4.5 53.3 1.0
N A:ASN189 4.5 45.5 1.0
C A:ASP181 4.5 56.4 1.0
CB A:HIS187 4.6 64.8 1.0
N A:ASP185 4.6 61.6 1.0
CB A:ASP185 4.7 63.8 1.0
CG A:ASP193 4.7 63.7 1.0
N A:GLY186 4.9 58.9 1.0
CB A:ASP183 5.0 46.5 1.0
C A:ILE188 5.0 54.9 1.0

Calcium binding site 2 out of 2 in 5o8x

Go back to Calcium Binding Sites List in 5o8x
Calcium binding site 2 out of 2 in the The X-Ray Structure of Catenated Lytic Transglycosylase SLTB1 From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The X-Ray Structure of Catenated Lytic Transglycosylase SLTB1 From Pseudomonas Aeruginosa within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca401

b:82.1
occ:1.00
O B:HIS187 2.3 69.6 1.0
OD1 B:ASP185 2.4 78.3 1.0
OD1 B:ASP181 2.5 59.6 1.0
OD2 B:ASP196 2.5 61.0 1.0
OD1 B:ASP183 2.6 66.4 1.0
OD1 B:ASP196 2.9 57.4 1.0
CG B:ASP196 3.1 59.6 1.0
CG B:ASP185 3.2 71.8 1.0
C B:HIS187 3.3 61.8 1.0
CG B:ASP181 3.4 69.5 1.0
OD2 B:ASP185 3.6 76.5 1.0
CG B:ASP183 3.7 65.6 1.0
OD2 B:ASP193 3.9 68.9 1.0
CA B:ASP181 3.9 57.3 1.0
N B:HIS187 3.9 67.1 1.0
CB B:ASP181 4.0 56.0 1.0
CA B:HIS187 4.1 60.5 1.0
N B:ILE188 4.2 62.0 1.0
OD2 B:ASP183 4.2 67.7 1.0
N B:PHE182 4.2 49.4 1.0
OD2 B:ASP181 4.3 76.1 1.0
CA B:ILE188 4.3 60.7 1.0
CB B:ASP185 4.4 71.8 1.0
N B:ASP183 4.4 46.5 1.0
C B:ASP181 4.4 55.7 1.0
N B:ASP185 4.4 61.6 1.0
CB B:ASP196 4.5 53.5 1.0
CB B:HIS187 4.6 63.1 1.0
N B:GLY186 4.6 63.3 1.0
N B:ASN189 4.6 52.1 1.0
CG B:ASP193 4.8 64.8 1.0
CA B:ASP185 4.8 72.0 1.0
N B:GLY184 4.9 63.7 1.0
CB B:ASP183 4.9 54.4 1.0
CA B:ASP183 5.0 55.5 1.0

Reference:

T.Dominguez-Gil, R.Molina, D.A.Dik, E.Spink, S.Mobashery, J.A.Hermoso. X-Ray Structure of Catenated Lytic Transglycosylase SLTB1. Biochemistry V. 56 6317 2017.
ISSN: ISSN 1520-4995
PubMed: 29131935
DOI: 10.1021/ACS.BIOCHEM.7B00932
Page generated: Mon Jul 15 09:44:06 2024

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