Calcium in PDB 1ai6: Penicillin Acylase with P-Hydroxyphenylacetic Acid

All present enzymatic activity of Penicillin Acylase with P-Hydroxyphenylacetic Acid:
3.5.1.11;

The structure of Penicillin Acylase with P-Hydroxyphenylacetic Acid, PDB code: 1ai6 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)	28.06 / 2.55
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 (%)	13.7 / 22

The binding sites of Calcium atom in the Penicillin Acylase with P-Hydroxyphenylacetic Acid (pdb code 1ai6). 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 with P-Hydroxyphenylacetic Acid, PDB code: 1ai6:

Calcium binding site 1 out of 1 in the Penicillin Acylase with P-Hydroxyphenylacetic Acid


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Penicillin Acylase with P-Hydroxyphenylacetic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca558 b:31.8 occ:1.00 OE2 A:GLU152 2.5 28.0 1.0 OD2 B:ASP73 2.6 30.5 1.0 OD2 B:ASP252 2.7 35.9 1.0 OD1 B:ASP76 2.7 29.6 1.0 O B:PRO205 2.7 36.5 1.0 O B:VAL75 2.8 38.7 1.0 OD1 B:ASP73 2.8 33.9 1.0 CG B:ASP73 3.1 27.6 1.0 CD A:GLU152 3.5 29.9 1.0 CG B:ASP76 3.5 30.6 1.0 CG B:ASP252 3.6 33.8 1.0 C B:VAL75 3.7 36.8 1.0 CA B:ASP76 3.7 35.6 1.0 C B:PRO205 3.8 34.5 1.0 CB B:ASP252 3.9 30.8 1.0 CB B:ASP76 4.0 25.9 1.0 CG A:GLU152 4.0 22.8 1.0 N B:ASP76 4.1 37.9 1.0 NH2 B:ARG199 4.1 28.7 1.0 O A:HOH219 4.1 27.8 1.0 O A:HOH212 4.2 29.3 1.0 CB B:PRO205 4.2 27.9 1.0 CA B:PRO205 4.3 32.8 1.0 OG1 A:THR150 4.4 27.6 1.0 CB B:ASP73 4.6 17.3 1.0 OE1 A:GLU152 4.6 30.5 1.0 OD2 B:ASP76 4.6 31.5 1.0 OD1 B:ASP252 4.7 32.5 1.0 N B:VAL75 4.8 28.5 1.0 N B:ARG206 4.8 35.1 1.0 CA B:VAL75 4.9 32.0 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