Calcium in PDB 1ai7: Penicillin Acylase Complexed with Phenol

All present enzymatic activity of Penicillin Acylase Complexed with Phenol:
3.5.1.11;

The structure of Penicillin Acylase Complexed with Phenol, PDB code: 1ai7 was solved by S.H.Done, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.97 / 2.50
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	52.120, 65.080, 76.300, 100.20, 111.44, 105.81
R / Rfree (%)	13.9 / 21.7

The binding sites of Calcium atom in the Penicillin Acylase Complexed with Phenol (pdb code 1ai7). 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 Complexed with Phenol, PDB code: 1ai7:

Calcium binding site 1 out of 1 in the Penicillin Acylase Complexed with Phenol


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Penicillin Acylase Complexed with Phenol within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca558 b:27.4 occ:1.00 OE2 A:GLU152 2.2 26.9 1.0 OD2 B:ASP73 2.2 31.7 1.0 OD2 B:ASP252 2.3 33.0 1.0 O B:PRO205 2.5 38.5 1.0 OD1 B:ASP76 2.6 32.3 1.0 OD1 B:ASP73 2.6 33.6 1.0 O B:VAL75 2.7 34.4 1.0 CG B:ASP73 2.9 25.8 1.0 CG B:ASP252 3.3 31.5 1.0 CD A:GLU152 3.4 29.8 1.0 CG B:ASP76 3.6 28.9 1.0 C B:PRO205 3.7 36.1 1.0 C B:VAL75 3.7 32.5 1.0 CB B:ASP252 3.8 26.0 1.0 CA B:ASP76 3.8 31.6 1.0 CG A:GLU152 3.9 16.1 1.0 CB B:ASP76 4.1 19.9 1.0 O A:HOH213 4.1 29.8 1.0 O B:HOH603 4.1 28.2 1.0 N B:ASP76 4.2 30.7 1.0 NH2 B:ARG199 4.2 29.4 1.0 CB B:PRO205 4.3 26.6 1.0 CA B:PRO205 4.3 30.8 1.0 CB B:ASP73 4.4 19.7 1.0 OD1 B:ASP252 4.4 30.2 1.0 OE1 A:GLU152 4.4 29.3 1.0 OG1 A:THR150 4.5 24.5 1.0 OD2 B:ASP76 4.6 31.0 1.0 N B:ARG206 4.7 36.8 1.0 N B:VAL75 4.9 26.0 1.0 CA B:VAL75 4.9 28.3 1.0 CA B:ARG206 4.9 31.6 1.0 O B:HOH675 5.0 36.9 1.0

S.H.Done, J.A.Brannigan, P.C.E.Moody, R.E.Hubbard. Ligand-Induced Conformational Change in Penicillin Acylase. J.Mol.Biol. V. 284 463 1998.
ISSN: ISSN 0022-2836
PubMed: 9813130
DOI: 10.1006/JMBI.1998.2180