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Calcium in PDB 1k5s: Penicillin Acylase, Mutant Complexed with Ppa

Enzymatic activity of Penicillin Acylase, Mutant Complexed with Ppa

All present enzymatic activity of Penicillin Acylase, Mutant Complexed with Ppa:
3.5.1.11;

Protein crystallography data

The structure of Penicillin Acylase, Mutant Complexed with Ppa, PDB code: 1k5s 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) 30.00 / 2.43
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 50.820, 64.360, 64.750, 72.89, 74.01, 73.55
R / Rfree (%) 17.3 / 23.3

Calcium Binding Sites:

The binding sites of Calcium atom in the Penicillin Acylase, Mutant Complexed with Ppa (pdb code 1k5s). 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 Complexed with Ppa, PDB code: 1k5s:

Calcium binding site 1 out of 1 in 1k5s

Go back to Calcium Binding Sites List in 1k5s
Calcium binding site 1 out of 1 in the Penicillin Acylase, Mutant Complexed with Ppa


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 Complexed with Ppa within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca558

b:15.6
occ:1.00
OE2 A:GLU152 2.2 13.4 1.0
OD1 B:ASP76 2.4 16.1 1.0
O B:VAL75 2.5 14.4 1.0
O B:PRO205 2.5 13.9 1.0
OD1 B:ASP73 2.6 14.5 1.0
OD2 B:ASP252 2.6 13.2 1.0
OD2 B:ASP73 2.7 13.7 1.0
CG B:ASP73 3.0 16.7 1.0
CD A:GLU152 3.4 15.0 1.0
C B:VAL75 3.6 15.0 1.0
CG B:ASP252 3.6 12.9 1.0
CG B:ASP76 3.6 18.1 1.0
C B:PRO205 3.6 14.0 1.0
CA B:ASP76 3.9 15.4 1.0
CB B:ASP252 3.9 13.7 1.0
O B:HOH628 3.9 12.7 1.0
CG A:GLU152 4.0 15.2 1.0
NH2 B:ARG199 4.1 17.2 1.0
N B:ASP76 4.1 15.0 1.0
CA B:PRO205 4.2 14.0 1.0
O A:HOH230 4.3 18.8 1.0
CB B:ASP76 4.3 15.0 1.0
OE1 A:GLU152 4.4 15.2 1.0
OG1 A:THR150 4.4 14.2 1.0
CB B:PRO205 4.5 12.9 1.0
OD2 B:ASP76 4.5 18.7 1.0
CB B:ASP73 4.6 16.0 1.0
N B:ARG206 4.7 14.5 1.0
OD1 B:ASP252 4.7 13.4 1.0
CA B:VAL75 4.7 15.1 1.0
N B:VAL75 4.8 15.2 1.0
O B:HOH772 4.9 30.6 1.0
CA B:ARG206 4.9 15.2 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: Mon Jul 7 16:19:06 2025

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