Cadmium in PDB 1x3g: Crystal Structure of the Single-Stranded Dna-Binding Protein From Mycobacterium Smegmatis

The structure of Crystal Structure of the Single-Stranded Dna-Binding Protein From Mycobacterium Smegmatis, PDB code: 1x3g was solved by K.Saikrishnan, G.P.Manjunath, P.Singh, J.Jeyakanthan, Z.Dauter, K.Sekar, K.Muniyappa, M.Vijayan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 3.00
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	79.886, 79.886, 81.288, 90.00, 90.00, 120.00
R / Rfree (%)	20.4 / 25.8

The binding sites of Cadmium atom in the Crystal Structure of the Single-Stranded Dna-Binding Protein From Mycobacterium Smegmatis (pdb code 1x3g). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total only one binding site of Cadmium was determined in the Crystal Structure of the Single-Stranded Dna-Binding Protein From Mycobacterium Smegmatis, PDB code: 1x3g:

Cadmium binding site 1 out of 1 in the Crystal Structure of the Single-Stranded Dna-Binding Protein From Mycobacterium Smegmatis


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Crystal Structure of the Single-Stranded Dna-Binding Protein From Mycobacterium Smegmatis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd1001 b:50.1 occ:1.00 OE1 A:GLU100 2.0 42.3 1.0 CD A:GLU100 2.3 37.0 1.0 OE2 A:GLU100 2.4 36.0 1.0 NH1 A:ARG56 3.4 41.6 1.0 CG A:GLU100 3.6 30.0 1.0 CZ A:ARG56 4.3 38.7 1.0 NH2 A:ARG56 4.4 42.2 1.0 CB A:GLU100 4.5 24.9 1.0 OD1 A:ASN58 4.8 20.2 1.0 CD A:ARG86 4.9 36.0 1.0 NH1 A:ARG86 5.0 44.2 1.0

K.Saikrishnan, G.P.Manjunath, P.Singh, J.Jeyakanthan, Z.Dauter, K.Sekar, K.Muniyappa, M.Vijayan. Structure of Mycobacterium Smegmatis Single-Stranded Dna-Binding Protein and A Comparative Study Involving Homologus Ssbs: Biological Implications of Structural Plasticity and Variability in Quaternary Association. Acta Crystallogr.,Sect.D V. 61 1140 2005.
ISSN: ISSN 0907-4449
PubMed: 16041080
DOI: 10.1107/S0907444905016896