Calcium in PDB 1fxv: Penicillin Acylase Mutant Impaired in Catalysis with Penicillin G in the Active Site

All present enzymatic activity of Penicillin Acylase Mutant Impaired in Catalysis with Penicillin G in the Active Site:
3.5.1.11;

The structure of Penicillin Acylase Mutant Impaired in Catalysis with Penicillin G in the Active Site, PDB code: 1fxv was solved by W.B.Alkema, C.M.Hensgens, E.H.Kroezinga, E.De Vries, R.Floris, J.M.Van Derlaan, B.W.Dijkstra, D.B.Janssen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.25
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	50.930, 63.966, 64.189, 72.85, 73.77, 74.06
R / Rfree (%)	18.7 / 23.6

The binding sites of Calcium atom in the Penicillin Acylase Mutant Impaired in Catalysis with Penicillin G in the Active Site (pdb code 1fxv). 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 Penicillin Acylase Mutant Impaired in Catalysis with Penicillin G in the Active Site, PDB code: 1fxv:

Calcium binding site 1 out of 1 in the Penicillin Acylase Mutant Impaired in Catalysis with Penicillin G in the Active Site


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Penicillin Acylase Mutant Impaired in Catalysis with Penicillin G in the Active Site within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca2001 b:11.2 occ:1.00 OE2 A:GLU152 2.3 8.5 1.0 OD1 B:ASP76 2.3 11.3 1.0 OD2 B:ASP252 2.4 7.0 1.0 O B:PRO205 2.4 13.2 1.0 O B:VAL75 2.5 10.8 1.0 OD2 B:ASP73 2.6 15.2 1.0 OD1 B:ASP73 2.7 8.2 1.0 CG B:ASP73 3.0 14.1 1.0 CD A:GLU152 3.4 11.5 1.0 CG B:ASP252 3.5 9.5 1.0 CG B:ASP76 3.5 14.4 1.0 C B:PRO205 3.6 12.0 1.0 C B:VAL75 3.6 12.3 1.0 CA B:ASP76 3.8 13.0 1.0 CB B:ASP252 3.9 11.8 1.0 O B:HOH2227 3.9 4.1 1.0 CG A:GLU152 3.9 8.0 1.0 O B:HOH2247 4.1 6.6 1.0 N B:ASP76 4.1 12.2 1.0 NH2 B:ARG199 4.1 9.9 1.0 CA B:PRO205 4.1 13.1 1.0 CB B:ASP76 4.2 13.3 1.0 CB B:PRO205 4.3 11.5 1.0 OG1 A:THR150 4.4 13.2 1.0 OD2 B:ASP76 4.5 12.9 1.0 OE1 A:GLU152 4.5 10.2 1.0 OD1 B:ASP252 4.6 8.7 1.0 CB B:ASP73 4.6 12.5 1.0 N B:ARG206 4.7 14.0 1.0 CA B:VAL75 4.8 12.1 1.0 N B:VAL75 4.9 13.8 1.0 CA B:ARG206 5.0 13.0 1.0 CZ B:ARG199 5.0 8.0 1.0

W.B.Alkema, C.M.Hensgens, E.H.Kroezinga, E.De Vries, R.Floris, J.M.Van Der Laan, B.W.Dijkstra, D.B.Janssen. Characterization of the Beta-Lactam Binding Site of Penicillin Acylase of Escherichia Coli By Structural and Site-Directed Mutagenesis Studies. Protein Eng. V. 13 857 2000.
ISSN: ISSN 0269-2139
PubMed: 11239085
DOI: 10.1093/PROTEIN/13.12.857