Calcium in PDB 2es4: Crystal Structure of the Burkholderia Glumae Lipase-Specific Foldase in Complex with Its Cognate Lipase

All present enzymatic activity of Crystal Structure of the Burkholderia Glumae Lipase-Specific Foldase in Complex with Its Cognate Lipase:
3.1.1.3;

The structure of Crystal Structure of the Burkholderia Glumae Lipase-Specific Foldase in Complex with Its Cognate Lipase, PDB code: 2es4 was solved by K.Pauwels, L.Wyns, J.Tommassen, S.N.Savvides, P.Van Gelder, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.85
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	183.000, 75.700, 116.600, 90.00, 117.60, 90.00
R / Rfree (%)	19.9 / 21.9

The structure of Crystal Structure of the Burkholderia Glumae Lipase-Specific Foldase in Complex with Its Cognate Lipase also contains other interesting chemical elements:

Iodine

(I)

8 atoms

The binding sites of Calcium atom in the Crystal Structure of the Burkholderia Glumae Lipase-Specific Foldase in Complex with Its Cognate Lipase (pdb code 2es4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the Burkholderia Glumae Lipase-Specific Foldase in Complex with Its Cognate Lipase, PDB code: 2es4:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of the Burkholderia Glumae Lipase-Specific Foldase in Complex with Its Cognate Lipase


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 Burkholderia Glumae Lipase-Specific Foldase in Complex with Its Cognate Lipase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca999 b:31.4 occ:1.00 O A:HOH1064 2.3 32.6 1.0 O A:VAL295 2.4 35.0 1.0 OD1 A:ASP287 2.4 27.0 1.0 O A:GLN291 2.5 26.6 1.0 O A:HOH1056 2.5 32.9 1.0 OD2 A:ASP241 2.5 41.3 1.0 C A:GLN291 3.4 26.7 1.0 CG A:ASP287 3.5 27.1 1.0 CG A:ASP241 3.5 45.4 1.0 C A:VAL295 3.6 34.5 1.0 N A:LEU292 3.7 27.7 1.0 CA A:ARG296 4.0 34.8 1.0 ND2 A:ASN284 4.1 32.5 1.0 OD2 A:ASP287 4.2 28.8 1.0 OD1 A:ASP241 4.2 43.5 1.0 OD1 A:ASN284 4.2 27.0 1.0 N A:ARG296 4.2 34.4 1.0 CA A:ASP287 4.3 23.3 1.0 N A:ASP287 4.3 22.1 1.0 CB A:ASP241 4.4 45.3 1.0 O A:HOH1073 4.4 36.0 1.0 OG A:SER243 4.5 43.1 1.0 CB A:ASP287 4.5 24.8 1.0 CB A:ARG296 4.5 35.2 1.0 OG1 A:THR244 4.6 35.6 1.0 CG A:ASN284 4.6 29.5 1.0 CA A:VAL295 4.7 34.3 1.0 C A:LEU286 4.7 22.9 1.0 CA A:GLN291 4.8 26.4 1.0 CB A:VAL295 4.9 33.9 1.0 CB A:LEU286 4.9 27.0 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of the Burkholderia Glumae Lipase-Specific Foldase in Complex with Its Cognate Lipase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the Burkholderia Glumae Lipase-Specific Foldase in Complex with Its Cognate Lipase within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca998 b:25.2 occ:1.00 OD1 B:ASP287 2.4 23.0 1.0 O B:GLN291 2.4 19.4 1.0 O B:VAL295 2.4 25.3 1.0 O B:HOH1066 2.5 25.2 1.0 OD2 B:ASP241 2.5 30.0 1.0 O B:HOH1087 2.5 27.0 1.0 C B:GLN291 3.4 20.0 1.0 CG B:ASP287 3.5 22.3 1.0 CG B:ASP241 3.6 30.9 1.0 C B:VAL295 3.6 26.1 1.0 N B:LEU292 3.6 22.0 1.0 CA B:ARG296 3.9 28.2 1.0 N B:ARG296 4.2 26.6 1.0 OD2 B:ASP287 4.3 18.9 1.0 O B:HOH1035 4.3 23.6 1.0 OD1 B:ASN284 4.4 16.9 1.0 N B:ASP287 4.4 16.5 1.0 CA B:ASP287 4.4 16.1 1.0 OD1 B:ASP241 4.4 33.0 1.0 CB B:ASP241 4.4 31.7 1.0 ND2 B:ASN284 4.5 16.7 1.0 OG B:SER243 4.5 29.6 1.0 CB B:ARG296 4.5 29.1 1.0 CB B:ASP287 4.5 17.6 1.0 OG1 B:THR244 4.7 24.9 1.0 CA B:VAL295 4.8 27.3 1.0 CA B:GLN291 4.8 18.9 1.0 C B:LEU286 4.8 19.4 1.0 CG B:ASN284 4.8 19.9 1.0 CB B:LEU286 4.9 22.5 1.0 CB B:VAL295 5.0 28.7 1.0

K.Pauwels, A.Lustig, L.Wyns, J.Tommassen, S.N.Savvides, P.Van Gelder. Structure of A Membrane-Based Steric Chaperone in Complex with Its Lipase Substrate. Nat.Struct.Mol.Biol. V. 13 374 2006.
ISSN: ISSN 1545-9993
PubMed: 16518399
DOI: 10.1038/NSMB1065