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Calcium in PDB 5lip: Pseudomonas Lipase Complexed with Rc-(Rp, Sp)-1,2- Dioctylcarbamoylglycero-3-O-Octylphosphonate

Enzymatic activity of Pseudomonas Lipase Complexed with Rc-(Rp, Sp)-1,2- Dioctylcarbamoylglycero-3-O-Octylphosphonate

All present enzymatic activity of Pseudomonas Lipase Complexed with Rc-(Rp, Sp)-1,2- Dioctylcarbamoylglycero-3-O-Octylphosphonate:
3.1.1.3;

Protein crystallography data

The structure of Pseudomonas Lipase Complexed with Rc-(Rp, Sp)-1,2- Dioctylcarbamoylglycero-3-O-Octylphosphonate, PDB code: 5lip was solved by D.A.Lang, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.730, 46.420, 83.950, 90.00, 121.23, 90.00
R / Rfree (%) 20.6 / 28.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Pseudomonas Lipase Complexed with Rc-(Rp, Sp)-1,2- Dioctylcarbamoylglycero-3-O-Octylphosphonate (pdb code 5lip). 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 Pseudomonas Lipase Complexed with Rc-(Rp, Sp)-1,2- Dioctylcarbamoylglycero-3-O-Octylphosphonate, PDB code: 5lip:

Calcium binding site 1 out of 1 in 5lip

Go back to Calcium Binding Sites List in 5lip
Calcium binding site 1 out of 1 in the Pseudomonas Lipase Complexed with Rc-(Rp, Sp)-1,2- Dioctylcarbamoylglycero-3-O-Octylphosphonate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Pseudomonas Lipase Complexed with Rc-(Rp, Sp)-1,2- Dioctylcarbamoylglycero-3-O-Octylphosphonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca321

b:8.7
occ:1.00
 O A:VAL296 2.5 7.2 1.0
OD1 A:ASP288 2.6 5.4 1.0
OD2 A:ASP242 2.8 6.9 1.0
O A:GLN292 3.1 5.7 1.0
CG A:ASP242 3.5 6.3 1.0
C A:VAL296 3.6 7.3 1.0
CG A:ASP288 3.8 3.1 1.0
OG1 A:THR245 3.9 3.8 1.0
OD1 A:ASP242 3.9 7.0 1.0
OD1 A:ASN285 4.2 7.8 1.0
CA A:ARG297 4.2 7.0 1.0
OG A:SER244 4.3 2.5 1.0
C A:GLN292 4.3 7.2 1.0
N A:ARG297 4.3 7.6 1.0
N A:ASP288 4.3 2.8 1.0
CA A:ASP288 4.4 3.0 1.0
CB A:ASP242 4.6 6.9 1.0
ND2 A:ASN285 4.6 7.2 1.0
OD2 A:ASP288 4.7 2.9 1.0
CA A:VAL296 4.7 5.9 1.0
CB A:ASP288 4.7 2.7 1.0
C A:LEU287 4.8 2.5 1.0
CG A:ASN285 4.8 5.7 1.0
CB A:LEU287 4.8 4.1 1.0
CB A:ARG297 4.8 6.2 1.0
CB A:LEU293 4.9 7.5 1.0
CB A:VAL296 4.9 4.0 1.0
O A:LEU293 4.9 10.4 1.0

Reference:

D.A.Lang, M.L.M.Mannesse, G.De Haas, H.M.Verheij, B.W.Dijkstra. Structural Basis of the Chiral Selectivity of Pseudomonas Cepacia Lipase Eur.J.Biochem. V. 254 333 1998.
ISSN: ISSN 0014-2956
PubMed: 9660188
DOI: 10.1046/J.1432-1327.1998.2540333.X
Page generated: Sat Dec 12 05:36:05 2020

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