Calcium in PDB 2erv: Crystal Structure of the Outer Membrane Enzyme Pagl

The structure of Crystal Structure of the Outer Membrane Enzyme Pagl, PDB code: 2erv was solved by L.Rutten, J.Geurtsen, W.Lambert, J.J.Smolenaers, A.M.Bonvin, P.Van Derley, M.R.Egmond, P.Gros, J.Tommassen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	92.264, 48.993, 105.026, 90.00, 115.46, 90.00
R / Rfree (%)	19.8 / 23.3

The binding sites of Calcium atom in the Crystal Structure of the Outer Membrane Enzyme Pagl (pdb code 2erv). 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 Crystal Structure of the Outer Membrane Enzyme Pagl, PDB code: 2erv:

Calcium binding site 1 out of 1 in the Crystal Structure of the Outer Membrane Enzyme Pagl


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Outer Membrane Enzyme Pagl within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca195 b:21.9 occ:1.00 O26 B:CXE1200 2.2 31.2 1.0 O23 B:CXE1200 2.4 33.1 1.0 O17 B:CXE1200 2.4 33.8 1.0 O14 B:CXE1200 2.4 34.5 1.0 OD2 B:ASP106 2.4 33.6 1.0 O20 B:CXE1200 2.4 25.8 1.0 OD2 A:ASP106 2.5 34.1 1.0 OD1 A:ASP106 3.0 34.0 1.0 CG A:ASP106 3.0 30.8 1.0 CG B:ASP106 3.1 28.9 1.0 OD1 B:ASP106 3.1 31.2 1.0 C25 B:CXE1200 3.3 32.1 1.0 C16 B:CXE1200 3.3 34.4 1.0 C24 B:CXE1200 3.4 34.0 1.0 C15 B:CXE1200 3.4 33.0 1.0 C21 B:CXE1200 3.4 25.3 1.0 C22 B:CXE1200 3.4 29.5 1.0 C19 B:CXE1200 3.4 27.3 1.0 C18 B:CXE1200 3.4 29.3 1.0 CB A:ASP106 4.3 28.0 1.0 CB B:ASP106 4.4 24.1 1.0 O11 B:CXE1100 4.9 49.0 1.0

L.Rutten, J.Geurtsen, W.Lambert, J.J.Smolenaers, A.M.Bonvin, A.De Haan, P.Van Der Ley, M.R.Egmond, P.Gros, J.Tommassen. Crystal Structure and Catalytic Mechanism of the Lps 3-O-Deacylase Pagl From Pseudomonas Aeruginosa. Proc.Natl.Acad.Sci.Usa V. 103 7071 2006.
ISSN: ISSN 0027-8424
PubMed: 16632613
DOI: 10.1073/PNAS.0509392103