Zinc in PDB 2wae: Penicillin-Binding Protein 2B (Pbp-2B) From Streptococcus Pneumoniae (Strain 5204)

The structure of Penicillin-Binding Protein 2B (Pbp-2B) From Streptococcus Pneumoniae (Strain 5204), PDB code: 2wae was solved by C.Contreras-Martel, C.Dahout-Gonzalez, A.Dos-Santos-Martins, M.Kotnik, A.Dessen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.39 / 2.26
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	127.951, 127.951, 280.847, 90.00, 90.00, 120.00
R / Rfree (%)	24.4 / 30.1

The binding sites of Zinc atom in the Penicillin-Binding Protein 2B (Pbp-2B) From Streptococcus Pneumoniae (Strain 5204) (pdb code 2wae). 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 Penicillin-Binding Protein 2B (Pbp-2B) From Streptococcus Pneumoniae (Strain 5204), PDB code: 2wae:

Zinc binding site 1 out of 1 in the Penicillin-Binding Protein 2B (Pbp-2B) From Streptococcus Pneumoniae (Strain 5204)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Penicillin-Binding Protein 2B (Pbp-2B) From Streptococcus Pneumoniae (Strain 5204) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1680 b:73.3 occ:0.50 OE2 A:GLU297 2.2 43.0 1.0 OE1 A:GLU284 2.2 34.4 1.0 NE2 A:HIS286 2.8 33.6 0.5 CE1 A:HIS286 3.0 30.9 0.5 CD A:GLU297 3.4 43.6 1.0 CD2 A:HIS286 3.4 32.7 0.5 CD A:GLU284 3.4 33.1 1.0 NE2 A:HIS286 3.7 29.7 0.5 ND1 A:HIS286 3.7 29.6 0.5 OE1 A:GLU297 4.0 41.8 1.0 CE1 A:HIS286 4.0 33.5 0.5 OE2 A:GLU284 4.1 32.7 1.0 CB A:GLU284 4.4 25.3 1.0 CG A:GLU297 4.5 42.8 1.0 CG A:GLU284 4.5 29.6 1.0 CG A:HIS286 4.7 31.3 0.5 CD2 A:HIS286 4.7 29.1 0.5 CG A:HIS286 4.7 29.5 0.5 OE1 A:GLN51 4.8 29.1 1.0 ND1 A:HIS286 4.9 32.9 0.5

C.Contreras-Martel, C.Dahout-Gonzalez, A.Dos-Santos-Martins, M.Kotnik, A.Dessen. Pbp Active Site Flexibility As the Key Mechanism For Beta-Lactam Resistance in Pneumococci J.Mol.Biol. V. 387 899 2009.
ISSN: ISSN 0022-2836
PubMed: 19233207
DOI: 10.1016/J.JMB.2009.02.024