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Calcium in PDB 2nw6: Burkholderia Cepacia Lipase Complexed with S-Inhibitor

Enzymatic activity of Burkholderia Cepacia Lipase Complexed with S-Inhibitor

All present enzymatic activity of Burkholderia Cepacia Lipase Complexed with S-Inhibitor:
3.1.1.3;

Protein crystallography data

The structure of Burkholderia Cepacia Lipase Complexed with S-Inhibitor, PDB code: 2nw6 was solved by M.Luic, Z.Stefanic, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.58 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 89.015, 46.584, 84.244, 90.00, 121.05, 90.00
R / Rfree (%) 17.5 / 21.3

Other elements in 2nw6:

The structure of Burkholderia Cepacia Lipase Complexed with S-Inhibitor also contains other interesting chemical elements:

Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Burkholderia Cepacia Lipase Complexed with S-Inhibitor (pdb code 2nw6). 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 Burkholderia Cepacia Lipase Complexed with S-Inhibitor, PDB code: 2nw6:

Calcium binding site 1 out of 1 in 2nw6

Go back to Calcium Binding Sites List in 2nw6
Calcium binding site 1 out of 1 in the Burkholderia Cepacia Lipase Complexed with S-Inhibitor


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Burkholderia Cepacia Lipase Complexed with S-Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca613

b:18.1
occ:1.00
O A:VAL296 2.4 17.4 1.0
OD2 A:ASP242 2.5 16.5 1.0
OD1 A:ASP288 2.5 13.8 1.0
O A:HOH619 2.6 15.8 1.0
O A:HOH638 2.6 15.5 1.0
O A:GLN292 3.2 27.8 1.0
C A:VAL296 3.6 15.8 1.0
CG A:ASP242 3.6 17.5 1.0
CG A:ASP288 3.7 15.5 1.0
CA A:ARG297 4.0 17.9 1.0
OG A:SER244 4.3 16.3 1.0
N A:ARG297 4.3 16.4 1.0
ND2 A:ASN285 4.3 15.4 1.0
CA A:ASP288 4.3 12.3 1.0
OD1 A:ASN285 4.3 15.7 1.0
O A:HOH712 4.4 14.5 1.0
N A:ASP288 4.4 12.3 1.0
C A:GLN292 4.4 27.4 1.0
OD2 A:ASP288 4.4 15.2 1.0
CB A:ASP242 4.4 15.4 1.0
OD1 A:ASP242 4.5 16.4 1.0
OG1 A:THR245 4.5 17.9 1.0
CB A:ARG297 4.6 17.6 1.0
CB A:ASP288 4.6 12.2 1.0
CA A:VAL296 4.7 16.8 1.0
C A:LEU287 4.7 13.7 1.0
CG A:ASN285 4.8 16.5 1.0
CB A:LEU293 4.8 29.8 1.0
CB A:VAL296 4.8 18.0 1.0
N A:VAL296 4.9 17.4 1.0
O A:LEU287 5.0 16.1 1.0
CB A:LEU287 5.0 16.9 1.0
CG1 A:VAL296 5.0 17.2 1.0

Reference:

M.Luic, Z.Stefanic, I.Ceilinger, M.Hodoscek, D.Janezic, T.Lenac, I.L.Asler, D.Sepac, S.Tomic. Combined X-Ray Diffraction and Qm/Mm Study of the Burkholderia Cepacia Lipase-Catalyzed Secondary Alcohol Esterification J.Phys.Chem.B V. 112 4876 2008.
ISSN: ISSN 1089-5647
PubMed: 18386861
DOI: 10.1021/JP077717U
Page generated: Sat Dec 12 03:48:01 2020

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