Calcium in PDB 1h2g: Altered Substrate Specificity Mutant of Penicillin Acylase

All present enzymatic activity of Altered Substrate Specificity Mutant of Penicillin Acylase:
3.5.1.11;

The structure of Altered Substrate Specificity Mutant of Penicillin Acylase, PDB code: 1h2g was solved by C.E.Mcvey, M.Morillas, J.A.Brannigan, A.G.Ladurner, L.J.Forney, R.Virden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.80 / 2.0
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	52.020, 64.230, 70.670, 70.58, 72.81, 73.84
R / Rfree (%)	15.2 / 19.4

The binding sites of Calcium atom in the Altered Substrate Specificity Mutant of Penicillin Acylase (pdb code 1h2g). 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 Altered Substrate Specificity Mutant of Penicillin Acylase, PDB code: 1h2g:

Calcium binding site 1 out of 1 in the Altered Substrate Specificity Mutant of Penicillin Acylase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Altered Substrate Specificity Mutant of Penicillin Acylase within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1558 b:12.3 occ:1.00 OE2 A:GLU152 2.3 10.5 1.0 OD2 B:ASP252 2.3 11.2 1.0 OD1 B:ASP76 2.4 9.9 1.0 O B:PRO205 2.4 12.4 1.0 O B:VAL75 2.5 11.4 1.0 OD2 B:ASP73 2.6 11.3 1.0 OD1 B:ASP73 2.6 11.4 1.0 CG B:ASP73 3.0 12.4 1.0 CG B:ASP252 3.4 11.8 1.0 CD A:GLU152 3.5 12.8 1.0 C B:VAL75 3.5 12.5 1.0 C B:PRO205 3.6 12.3 1.0 CG B:ASP76 3.6 12.4 1.0 CA B:ASP76 3.8 12.5 1.0 CB B:ASP252 3.8 11.9 1.0 CG A:GLU152 4.0 11.9 1.0 NH2 B:ARG199 4.0 13.9 1.0 N B:ASP76 4.1 13.1 1.0 O B:HOH2155 4.1 12.6 1.0 O A:HOH2119 4.1 18.9 1.0 CA B:PRO205 4.2 12.6 1.0 CB B:ASP76 4.2 13.0 1.0 CB B:PRO205 4.2 12.9 1.0 OD1 B:ASP252 4.5 11.7 1.0 CB B:ASP73 4.5 11.7 1.0 OE1 A:GLU152 4.5 11.9 1.0 OD2 B:ASP76 4.6 10.3 1.0 N B:ARG206 4.6 12.3 1.0 CA B:VAL75 4.7 12.5 1.0 N B:VAL75 4.7 11.9 1.0 CA B:ARG206 4.9 12.8 1.0 O B:HOH2044 5.0 22.9 1.0 N B:ASP252 5.0 11.9 1.0 OG1 A:THR150 5.0 15.4 1.0 CZ B:ARG199 5.0 13.7 1.0

M.Morillas, C.E.Mcvey, J.A.Brannigan, A.G.Ladurner, L.J.Forney, R.Virden. Mutations of Penicillin Acylase Residue B71 Extend Substrate Specificity By Decreasing Steric Constraints For Substrate Binding Biochem.J. V. 371 143 2003.
ISSN: ISSN 0264-6021
PubMed: 12511194
DOI: 10.1042/BJ20021383