Calcium in PDB 1zja: Crystal Structure of the Trehalulose Synthase Mutb From Pseudomonas Mesoacidophila Mx-45 (Triclinic Form)

All present enzymatic activity of Crystal Structure of the Trehalulose Synthase Mutb From Pseudomonas Mesoacidophila Mx-45 (Triclinic Form):
5.4.99.11;

The structure of Crystal Structure of the Trehalulose Synthase Mutb From Pseudomonas Mesoacidophila Mx-45 (Triclinic Form), PDB code: 1zja was solved by S.Ravaud, X.Robert, R.Haser, N.Aghajari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.00 / 1.60
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	63.670, 71.960, 82.240, 67.36, 73.13, 70.82
R / Rfree (%)	18.4 / 21.9

The binding sites of Calcium atom in the Crystal Structure of the Trehalulose Synthase Mutb From Pseudomonas Mesoacidophila Mx-45 (Triclinic Form) (pdb code 1zja). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the Trehalulose Synthase Mutb From Pseudomonas Mesoacidophila Mx-45 (Triclinic Form), PDB code: 1zja:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of the Trehalulose Synthase Mutb From Pseudomonas Mesoacidophila Mx-45 (Triclinic Form)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Trehalulose Synthase Mutb From Pseudomonas Mesoacidophila Mx-45 (Triclinic Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca7001 b:8.8 occ:1.00 O A:ILE28 2.3 12.2 1.0 OD1 A:ASP22 2.4 11.9 1.0 OD2 A:ASP30 2.4 12.9 1.0 OD1 A:ASP26 2.4 12.4 1.0 OD1 A:ASN24 2.4 15.3 1.0 O A:HOH4715 2.4 14.3 1.0 O A:HOH4531 2.6 17.5 1.0 CG A:ASP26 3.3 9.9 1.0 CG A:ASP22 3.4 10.6 1.0 CG A:ASN24 3.4 18.0 1.0 CG A:ASP30 3.5 8.5 1.0 C A:ILE28 3.5 10.7 1.0 OD2 A:ASP26 3.7 16.6 1.0 CB A:ASP30 3.9 8.4 1.0 ND2 A:ASN24 4.0 18.5 1.0 OD2 A:ASP22 4.1 10.7 1.0 N A:THR23 4.2 9.4 1.0 N A:ASN24 4.2 12.2 1.0 N A:ILE28 4.2 10.4 1.0 O A:GLU75 4.3 12.0 1.0 CB A:ASP22 4.3 9.9 1.0 CA A:ASP22 4.3 11.2 1.0 CA A:ILE28 4.3 9.8 1.0 C A:GLY29 4.3 8.1 1.0 O A:GLY29 4.5 8.2 1.0 N A:GLY29 4.5 9.6 1.0 CB A:ASP26 4.5 14.6 1.0 CB A:ILE28 4.6 9.3 1.0 OD1 A:ASP30 4.6 7.2 1.0 CB A:ASN24 4.6 15.3 1.0 N A:ASP26 4.6 11.7 1.0 N A:ASP30 4.6 8.3 1.0 CA A:GLY29 4.6 6.7 1.0 C A:ASP22 4.8 10.4 1.0 O A:HOH5510 4.8 23.8 1.0 CA A:ASN24 4.8 15.9 1.0 CA A:ASP30 4.9 6.2 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of the Trehalulose Synthase Mutb From Pseudomonas Mesoacidophila Mx-45 (Triclinic Form)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the Trehalulose Synthase Mutb From Pseudomonas Mesoacidophila Mx-45 (Triclinic Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca7000 b:10.1 occ:1.00 OD1 B:ASP22 2.3 13.0 1.0 OD1 B:ASN24 2.3 15.7 1.0 O B:ILE28 2.4 10.3 1.0 OD2 B:ASP30 2.4 12.6 1.0 O B:HOH4405 2.4 17.9 1.0 OD1 B:ASP26 2.5 12.1 1.0 O B:HOH4097 2.6 18.0 1.0 CG B:ASP26 3.3 12.4 1.0 CG B:ASP22 3.4 10.6 1.0 CG B:ASN24 3.4 19.3 1.0 CG B:ASP30 3.5 11.3 1.0 C B:ILE28 3.6 10.3 1.0 OD2 B:ASP26 3.6 19.4 1.0 CB B:ASP30 3.9 11.4 1.0 OD2 B:ASP22 4.1 14.0 1.0 ND2 B:ASN24 4.1 20.7 1.0 N B:ASN24 4.2 14.4 1.0 N B:THR23 4.2 11.9 1.0 N B:ILE28 4.2 8.5 1.0 CB B:ASP22 4.3 10.1 1.0 CA B:ASP22 4.3 11.6 1.0 CA B:ILE28 4.3 10.7 1.0 O B:GLU75 4.4 11.1 1.0 C B:GLY29 4.4 9.4 1.0 CB B:ASN24 4.5 16.1 1.0 O B:GLY29 4.5 9.2 1.0 N B:ASP26 4.5 11.9 1.0 CB B:ASP26 4.5 10.9 1.0 CB B:ILE28 4.5 10.9 1.0 OD1 B:ASP30 4.6 12.8 1.0 N B:ASP30 4.6 8.8 1.0 N B:GLY29 4.6 8.8 1.0 CA B:GLY29 4.7 8.4 1.0 C B:ASP22 4.7 10.5 1.0 CA B:ASN24 4.7 16.5 1.0 O B:HOH5044 4.8 21.0 1.0 O B:HOH4625 4.9 25.1 1.0 CA B:ASP30 4.9 11.0 1.0 C B:ASN24 4.9 16.0 1.0 N B:GLY25 5.0 15.4 1.0 CA B:ASP26 5.0 10.7 1.0

S.Ravaud, X.Robert, H.Watzlawick, R.Haser, R.Mattes, N.Aghajari. Trehalulose Synthase Native and Carbohydrate Complexed Structures Provide Insights Into Sucrose Isomerization. J.Biol.Chem. V. 282 28126 2007.
ISSN: ISSN 0021-9258
PubMed: 17597061
DOI: 10.1074/JBC.M704515200