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Calcium in PDB 4gin: Crystal Structure of the Mutb R284C Mutant From Crystals Soaked with the Inhibitor Deoxynojirimycin

Enzymatic activity of Crystal Structure of the Mutb R284C Mutant From Crystals Soaked with the Inhibitor Deoxynojirimycin

All present enzymatic activity of Crystal Structure of the Mutb R284C Mutant From Crystals Soaked with the Inhibitor Deoxynojirimycin:
5.4.11.99;

Protein crystallography data

The structure of Crystal Structure of the Mutb R284C Mutant From Crystals Soaked with the Inhibitor Deoxynojirimycin, PDB code: 4gin was solved by A.Lipski, 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) 44.85 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 83.800, 89.700, 91.600, 90.00, 90.00, 90.00
R / Rfree (%) 14 / 18.1

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Mutb R284C Mutant From Crystals Soaked with the Inhibitor Deoxynojirimycin (pdb code 4gin). 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 Crystal Structure of the Mutb R284C Mutant From Crystals Soaked with the Inhibitor Deoxynojirimycin, PDB code: 4gin:

Calcium binding site 1 out of 1 in 4gin

Go back to Calcium Binding Sites List in 4gin
Calcium binding site 1 out of 1 in the Crystal Structure of the Mutb R284C Mutant From Crystals Soaked with the Inhibitor Deoxynojirimycin


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 Mutb R284C Mutant From Crystals Soaked with the Inhibitor Deoxynojirimycin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca601

b:13.4
occ:1.00
 O A:HOH860 2.3 24.1 1.0
OD1 A:ASN24 2.3 16.8 1.0
OD1 A:ASP26 2.4 15.6 1.0
OD1 A:ASP22 2.4 12.8 1.0
O A:ILE28 2.4 10.9 1.0
OD2 A:ASP30 2.5 13.4 1.0
O A:HOH859 2.5 21.5 1.0
CG A:ASP26 3.2 17.8 1.0
OD2 A:ASP26 3.3 18.8 1.0
CG A:ASP22 3.4 12.9 1.0
CG A:ASN24 3.4 23.2 1.0
CG A:ASP30 3.5 16.6 1.0
C A:ILE28 3.6 13.9 1.0
CB A:ASP30 3.9 11.6 1.0
ND2 A:ASN24 4.1 21.8 1.0
N A:ASN24 4.2 15.2 1.0
OD2 A:ASP22 4.2 14.6 1.0
N A:ILE28 4.2 11.6 1.0
N A:THR23 4.2 10.3 1.0
CB A:ASP22 4.3 10.4 1.0
CA A:ILE28 4.3 14.2 1.0
CA A:ASP22 4.3 9.9 1.0
CB A:ILE28 4.4 15.2 1.0
C A:GLY29 4.4 13.2 1.0
CB A:ASP26 4.5 17.6 1.0
CB A:ASN24 4.5 20.0 1.0
N A:ASP26 4.5 11.6 1.0
O A:GLU75 4.6 18.4 1.0
O A:GLY29 4.6 10.1 1.0
N A:GLY29 4.6 12.4 1.0
OD1 A:ASP30 4.6 12.6 1.0
N A:ASP30 4.6 9.0 1.0
C A:ASP22 4.7 14.6 1.0
CA A:ASN24 4.7 17.0 1.0
CA A:GLY29 4.8 8.8 1.0
O A:HOH1266 4.8 42.9 1.0
CA A:ASP30 4.9 9.1 1.0
CA A:ASP26 4.9 15.8 1.0
N A:GLY25 5.0 14.1 1.0
C A:ASN24 5.0 18.4 1.0

Reference:

A.Lipski, H.Watzlawick, S.Ravaud, X.Robert, M.Rhimi, R.Haser, R.Mattes, N.Aghajari. Mutations Inducing An Active-Site Aperture in Rhizobium Sp. Sucrose Isomerase Confer Hydrolytic Activity Acta Crystallogr.,Sect.D V. 69 298 2013.
ISSN: ISSN 0907-4449
PubMed: 23385465
DOI: 10.1107/S0907444912045532
Page generated: Tue Jul 8 20:21:10 2025

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