Nickel in PDB 3cgm: Crystal Structure of Thermophilic Slyd

All present enzymatic activity of Crystal Structure of Thermophilic Slyd:
5.2.1.8;

The structure of Crystal Structure of Thermophilic Slyd, PDB code: 3cgm was solved by C.Loew, P.Neumann, M.T.Stubbs, J.Balbach, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.27 / 2.41
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	121.780, 121.780, 76.260, 90.00, 90.00, 120.00
R / Rfree (%)	18.7 / 22.6

The binding sites of Nickel atom in the Crystal Structure of Thermophilic Slyd (pdb code 3cgm). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Crystal Structure of Thermophilic Slyd, PDB code: 3cgm:

Nickel binding site 1 out of 1 in the Crystal Structure of Thermophilic Slyd


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of Thermophilic Slyd within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni164 b:35.5 occ:1.00 NE2 A:HIS157 2.0 40.7 1.0 ND1 A:HIS145 2.2 37.4 1.0 NE2 A:HIS149 2.2 35.6 1.0 NE2 A:HIS147 2.3 39.1 1.0 NE2 A:HIS155 2.3 31.9 1.0 CE1 A:HIS145 2.9 40.7 1.0 CE1 A:HIS157 3.0 40.1 1.0 CD2 A:HIS157 3.1 40.0 1.0 CD2 A:HIS149 3.1 34.8 1.0 CE1 A:HIS147 3.2 38.6 1.0 CE1 A:HIS155 3.3 30.0 1.0 CE1 A:HIS149 3.3 35.6 1.0 CD2 A:HIS155 3.3 32.9 1.0 CD2 A:HIS147 3.3 36.1 1.0 CG A:HIS145 3.3 38.0 1.0 CB A:HIS145 3.8 35.2 1.0 ND1 A:HIS157 4.1 42.8 1.0 NE2 A:HIS145 4.1 40.6 1.0 CG A:HIS157 4.2 42.7 1.0 CG A:HIS149 4.3 35.3 1.0 ND1 A:HIS149 4.3 35.6 1.0 CD2 A:HIS145 4.3 39.2 1.0 ND1 A:HIS147 4.3 38.4 1.0 ND1 A:HIS155 4.4 34.1 1.0 CG A:HIS147 4.4 35.9 1.0 CG A:HIS155 4.4 36.1 1.0

C.Loew, P.Neumann, H.Tidow, U.Weininger, C.Haupt, B.Friedrich-Epler, C.Scholz, M.T.Stubbs, J.Balbach. Crystal Structure Determination and Functional Characterization of the Metallochaperone Slyd From Thermus Thermophilus J.Mol.Biol. V. 398 375 2010.
ISSN: ISSN 0022-2836
PubMed: 20230833
DOI: 10.1016/J.JMB.2010.03.014