Zinc in PDB 4npe: High-Resolution Structure of C Domain of Staphylococcal Protein A at Room Temperature

The structure of High-Resolution Structure of C Domain of Staphylococcal Protein A at Room Temperature, PDB code: 4npe was solved by L.N.Deis, C.W.Pemble Iv, T.G.Oas, J.S.Richardson, D.C.Richardson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.52 / 1.42
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	27.840, 38.560, 28.960, 90.00, 118.20, 90.00
R / Rfree (%)	11.1 / 14.3

The binding sites of Zinc atom in the High-Resolution Structure of C Domain of Staphylococcal Protein A at Room Temperature (pdb code 4npe). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the High-Resolution Structure of C Domain of Staphylococcal Protein A at Room Temperature, PDB code: 4npe:

Zinc binding site 1 out of 1 in the High-Resolution Structure of C Domain of Staphylococcal Protein A at Room Temperature


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of High-Resolution Structure of C Domain of Staphylococcal Protein A at Room Temperature within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn101 b:12.7 occ:1.00 OXT A:LYS58 1.9 19.1 0.3 N A:SCN102 1.9 18.4 1.0 OXT A:LYS58 1.9 14.6 0.7 C A:LYS58 2.7 19.7 0.3 O A:LYS58 2.8 20.2 0.3 C A:LYS58 2.8 14.4 0.7 O A:LYS58 3.0 15.1 0.7 C A:SCN102 3.0 17.9 1.0 HG3 A:LYS58 4.0 28.5 0.7 CA A:LYS58 4.1 20.5 0.3 O A:HOH246 4.2 35.7 1.0 CA A:LYS58 4.2 15.8 0.7 HA A:LYS58 4.3 20.5 0.3 HB2 A:LYS58 4.4 25.4 0.7 HA A:LYS58 4.4 20.5 0.7 HB2 A:LYS58 4.6 25.4 0.3 CB A:LYS58 4.7 23.1 0.7 S A:SCN102 4.7 21.7 1.0 HG3 A:LYS58 4.7 28.5 0.3 CG A:LYS58 4.8 28.0 0.7 CB A:LYS58 4.9 25.4 0.3 H A:LYS58 5.0 18.1 0.3

L.N.Deis, C.W.Pemble, Y.Qi, A.Hagarman, D.C.Richardson, J.S.Richardson, T.G.Oas. Multiscale Conformational Heterogeneity in Staphylococcal Protein A: Possible Determinant of Functional Plasticity. Structure V. 22 1467 2014.
ISSN: ISSN 0969-2126
PubMed: 25295398
DOI: 10.1016/J.STR.2014.08.014