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Calcium in PDB 1kec: Penicillin Acylase Mutant with Phenyl Proprionic Acid

Enzymatic activity of Penicillin Acylase Mutant with Phenyl Proprionic Acid

All present enzymatic activity of Penicillin Acylase Mutant with Phenyl Proprionic Acid:
3.5.1.11;

Protein crystallography data

The structure of Penicillin Acylase Mutant with Phenyl Proprionic Acid, PDB code: 1kec was solved by C.M.H.Hensgens, E.Keizer, H.J.Snijder, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.14 / 2.30
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 50.781, 64.226, 64.543, 72.60, 73.86, 73.56
R / Rfree (%) 15.1 / 20.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Penicillin Acylase Mutant with Phenyl Proprionic Acid (pdb code 1kec). 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 with Phenyl Proprionic Acid, PDB code: 1kec:

Calcium binding site 1 out of 1 in 1kec

Go back to Calcium Binding Sites List in 1kec
Calcium binding site 1 out of 1 in the Penicillin Acylase Mutant with Phenyl Proprionic 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 Mutant with Phenyl Proprionic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca702

b:14.0
occ:1.00
OE2 A:GLU152 2.2 10.6 1.0
OD2 B:ASP252 2.4 9.4 1.0
O B:VAL75 2.5 11.3 1.0
OD1 B:ASP76 2.5 9.3 1.0
O B:PRO205 2.5 10.6 1.0
OD2 B:ASP73 2.6 12.9 1.0
OD1 B:ASP73 2.6 11.2 1.0
CG B:ASP73 3.0 11.6 1.0
CD A:GLU152 3.4 11.4 1.0
CG B:ASP252 3.4 10.8 1.0
C B:VAL75 3.5 11.4 1.0
CG B:ASP76 3.7 12.2 1.0
C B:PRO205 3.7 10.4 1.0
CA B:ASP76 3.8 11.8 1.0
CB B:ASP252 3.8 11.1 1.0
CG A:GLU152 4.0 11.4 1.0
O B:HOH732 4.0 9.3 1.0
O B:HOH816 4.0 14.2 1.0
NH2 B:ARG199 4.1 9.7 1.0
N B:ASP76 4.1 11.8 1.0
CB B:ASP76 4.2 11.5 1.0
OG1 A:THR150 4.3 12.5 1.0
CA B:PRO205 4.3 10.1 1.0
OE1 A:GLU152 4.4 12.4 1.0
CB B:PRO205 4.5 9.5 1.0
OD1 B:ASP252 4.5 10.3 1.0
CB B:ASP73 4.5 10.4 1.0
OD2 B:ASP76 4.7 11.8 1.0
CA B:VAL75 4.7 10.9 1.0
N B:ARG206 4.7 10.4 1.0
N B:VAL75 4.8 10.7 1.0
O B:HOH959 4.9 17.9 1.0
CA B:ARG206 4.9 10.9 1.0
CZ B:ARG199 5.0 9.4 1.0

Reference:

W.B.L.Alkema, C.M.H.Hensgens, H.J.Snijder, E.Keizer, B.W.Dijkstra, D.B.Janssen. Structural and Kinetic Studies on Ligand Binding in Wild-Type and Active-Site Mutants of Penicillin Acylase. Protein Eng.Des.Sel. V. 17 473 2004.
ISSN: ISSN 1741-0126
PubMed: 15254299
DOI: 10.1093/PROTEIN/GZH057
Page generated: Sat Dec 12 03:03:42 2020

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