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Calcium in PDB 1fxh: Mutant of Penicillin Acylase Impaired in Catalysis with Phenylacetic Acid in the Active Site

Enzymatic activity of Mutant of Penicillin Acylase Impaired in Catalysis with Phenylacetic Acid in the Active Site

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

Protein crystallography data

The structure of Mutant of Penicillin Acylase Impaired in Catalysis with Phenylacetic Acid in the Active Site, PDB code: 1fxh was solved by 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, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.97
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 51.014, 64.084, 64.225, 72.92, 73.91, 73.54
R / Rfree (%) 18.1 / 21.5

Calcium Binding Sites:

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

Calcium binding site 1 out of 1 in 1fxh

Go back to Calcium Binding Sites List in 1fxh
Calcium binding site 1 out of 1 in the Mutant of Penicillin Acylase Impaired in Catalysis with Phenylacetic Acid 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 Mutant of Penicillin Acylase Impaired in Catalysis with Phenylacetic Acid in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1002

b:9.1
occ:1.00
 OE2 A:GLU152 2.2 8.2 1.0
OD1 B:ASP76 2.3 8.0 1.0
OD2 B:ASP252 2.4 6.7 1.0
O B:VAL75 2.5 7.4 1.0
O B:PRO205 2.5 9.3 1.0
OD2 B:ASP73 2.6 9.7 1.0
OD1 B:ASP73 2.6 9.0 1.0
CG B:ASP73 3.0 9.6 1.0
CD A:GLU152 3.4 8.8 1.0
CG B:ASP252 3.5 5.2 1.0
C B:VAL75 3.5 6.9 1.0
CG B:ASP76 3.5 10.2 1.0
C B:PRO205 3.6 9.2 1.0
CA B:ASP76 3.8 7.5 1.0
CB B:ASP252 3.8 8.3 1.0
CG A:GLU152 3.9 7.9 1.0
O B:HOH1270 4.0 6.5 1.0
N B:ASP76 4.0 6.9 1.0
O A:HOH213 4.1 12.7 1.0
NH2 B:ARG199 4.1 10.0 1.0
CA B:PRO205 4.1 9.3 1.0
CB B:ASP76 4.2 8.1 1.0
CB B:PRO205 4.3 8.9 1.0
OG1 A:THR150 4.4 10.1 1.0
OE1 A:GLU152 4.4 7.7 1.0
OD2 B:ASP76 4.5 8.8 1.0
CB B:ASP73 4.5 9.7 1.0
OD1 B:ASP252 4.6 7.0 1.0
CA B:VAL75 4.7 7.3 1.0
N B:ARG206 4.7 9.8 1.0
N B:VAL75 4.7 7.3 1.0
CZ B:ARG199 5.0 11.4 1.0

Reference:

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
Page generated: Mon Jul 7 14:57:54 2025

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