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Calcium in PDB 1lpa: Interfacial Activation of the Lipase-Procolipase Complex By Mixed Micelles Revealed By X-Ray Crystallography

Enzymatic activity of Interfacial Activation of the Lipase-Procolipase Complex By Mixed Micelles Revealed By X-Ray Crystallography

All present enzymatic activity of Interfacial Activation of the Lipase-Procolipase Complex By Mixed Micelles Revealed By X-Ray Crystallography:
3.1.1.3;

Protein crystallography data

The structure of Interfacial Activation of the Lipase-Procolipase Complex By Mixed Micelles Revealed By X-Ray Crystallography, PDB code: 1lpa was solved by H.Van Tilbeurgh, M.-P.Egloff, C.Cambillau, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 3.04
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 133.400, 133.400, 92.600, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Interfacial Activation of the Lipase-Procolipase Complex By Mixed Micelles Revealed By X-Ray Crystallography (pdb code 1lpa). 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 Interfacial Activation of the Lipase-Procolipase Complex By Mixed Micelles Revealed By X-Ray Crystallography, PDB code: 1lpa:

Calcium binding site 1 out of 1 in 1lpa

Go back to Calcium Binding Sites List in 1lpa
Calcium binding site 1 out of 1 in the Interfacial Activation of the Lipase-Procolipase Complex By Mixed Micelles Revealed By X-Ray Crystallography


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Interfacial Activation of the Lipase-Procolipase Complex By Mixed Micelles Revealed By X-Ray Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca451

b:29.2
occ:1.00
 O B:GLU187 1.6 19.0 1.0
O B:ARG190 1.6 8.2 1.0
OD1 B:ASP195 2.3 9.6 1.0
OD2 B:ASP195 2.4 2.0 1.0
OD1 B:ASP192 2.6 13.4 1.0
CG B:ASP195 2.7 4.2 1.0
C B:GLU187 2.9 11.9 1.0
C B:ARG190 2.9 4.1 1.0
CG B:ASP192 3.7 10.9 1.0
O B:LEU188 3.8 8.8 1.0
N B:LEU188 3.9 9.3 1.0
N B:LEU191 3.9 2.0 1.0
CA B:GLU187 3.9 12.1 1.0
CA B:ARG190 4.0 4.1 1.0
N B:ARG190 4.1 4.0 1.0
C B:LEU188 4.2 7.0 1.0
CA B:LEU191 4.2 2.0 1.0
O B:GLY159 4.2 11.4 1.0
CA B:LEU188 4.2 6.3 1.0
N B:ASP192 4.2 3.9 1.0
CB B:ASP195 4.3 3.3 1.0
C B:LEU191 4.4 3.2 1.0
CB B:GLU187 4.4 19.4 1.0
CB B:ASP192 4.5 6.0 1.0
OD2 B:ASP192 4.6 19.7 1.0
CG B:ARG163 4.8 6.4 1.0
C B:GLY159 4.8 8.4 1.0
CD B:ARG163 4.9 9.9 1.0
O B:ASP192 4.9 2.2 1.0
N B:VAL189 4.9 6.4 1.0
CA B:ASP192 5.0 2.0 1.0
CB B:ARG163 5.0 3.2 1.0

Reference:

H.Van Tilbeurgh, M.P.Egloff, C.Martinez, N.Rugani, R.Verger, C.Cambillau. Interfacial Activation of the Lipase-Procolipase Complex By Mixed Micelles Revealed By X-Ray Crystallography. Nature V. 362 814 1993.
ISSN: ISSN 0028-0836
PubMed: 8479519
DOI: 10.1038/362814A0
Page generated: Mon Jul 7 16:57:45 2025

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