Calcium in PDB 1kkm: L.Casei Hprk/P in Complex with B.Subtilis P-Ser-Hpr

The structure of L.Casei Hprk/P in Complex with B.Subtilis P-Ser-Hpr, PDB code: 1kkm was solved by S.Fieulaine, S.Morera, S.Poncet, A.Galinier, J.Janin, J.Deutscher, S.Nessler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.80
Space group	P 32 1 2
Cell size a, b, c (Å), α, β, γ (°)	80.832, 80.832, 252.488, 90.00, 90.00, 120.00
R / Rfree (%)	20 / 25.7

The binding sites of Calcium atom in the L.Casei Hprk/P in Complex with B.Subtilis P-Ser-Hpr (pdb code 1kkm). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the L.Casei Hprk/P in Complex with B.Subtilis P-Ser-Hpr, PDB code: 1kkm:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the L.Casei Hprk/P in Complex with B.Subtilis P-Ser-Hpr


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of L.Casei Hprk/P in Complex with B.Subtilis P-Ser-Hpr within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:57.5 occ:1.00 OE1 A:GLU204 2.7 49.0 1.0 O1P H:SEP46 2.7 64.4 1.0 O A:GLU204 2.8 43.0 1.0 OG A:SER162 2.9 49.8 1.0 CB A:SER162 3.5 46.5 1.0 O3 A:PO4501 3.5 97.0 1.0 CD A:GLU204 3.7 48.9 1.0 P H:SEP46 3.8 65.4 1.0 O3P H:SEP46 3.8 66.8 1.0 C A:GLU204 3.8 43.9 1.0 CB A:GLU204 4.2 44.6 1.0 NH2 C:ARG245 4.3 56.0 1.0 OE2 A:GLU204 4.4 50.2 1.0 P A:PO4501 4.5 96.2 1.0 O1 A:PO4501 4.5 97.4 1.0 CA A:GLU204 4.5 42.5 1.0 CG A:GLU204 4.6 46.0 1.0 O A:HOH533 4.6 56.1 1.0 N A:SER162 4.6 43.1 1.0 CA A:SER162 4.7 44.8 1.0 O4 A:PO4501 4.7 98.1 1.0 OE1 A:GLU163 4.7 48.3 1.0 OG H:SEP46 4.7 63.9 1.0 OD1 A:ASP178 4.8 47.3 1.0 N A:GLU204 4.8 40.7 1.0 N A:ILE205 4.8 45.0 1.0 OE2 A:GLU163 4.9 48.0 1.0 O2P H:SEP46 4.9 64.3 1.0 OD2 A:ASP178 5.0 43.5 1.0

Calcium binding site 2 out of 3 in the L.Casei Hprk/P in Complex with B.Subtilis P-Ser-Hpr


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of L.Casei Hprk/P in Complex with B.Subtilis P-Ser-Hpr within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca402 b:48.9 occ:1.00 O1P I:SEP46 2.8 72.2 0.8 OE1 B:GLU204 2.8 50.1 1.0 OG B:SER162 2.8 43.7 1.0 O B:GLU204 2.9 37.9 1.0 O B:HOH550 3.0 37.9 1.0 CB B:SER162 3.2 42.2 1.0 O1 B:PO4502 3.7 41.6 0.0 O3 B:PO4502 3.8 42.3 0.8 CD B:GLU204 3.8 49.6 1.0 C B:GLU204 4.0 38.1 1.0 P I:SEP46 4.1 72.4 0.8 P B:PO4502 4.3 39.3 0.8 NH2 A:ARG245 4.3 80.2 1.0 CB B:GLU204 4.3 45.3 1.0 N B:SER162 4.4 35.7 1.0 CA B:SER162 4.4 36.9 1.0 OE2 B:GLU204 4.5 50.6 1.0 O3P I:SEP46 4.5 73.3 0.8 OE1 B:GLU163 4.6 45.8 1.0 OE2 B:GLU163 4.6 44.6 1.0 O4 B:PO4502 4.6 43.0 0.8 CA B:GLU204 4.7 36.4 1.0 CG B:GLU204 4.7 47.9 1.0 OD1 B:ASP178 4.9 41.1 1.0 N B:GLU204 4.9 34.5 1.0 N B:ILE205 5.0 52.8 1.0 OD2 B:ASP178 5.0 40.7 1.0

Calcium binding site 3 out of 3 in the L.Casei Hprk/P in Complex with B.Subtilis P-Ser-Hpr


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of L.Casei Hprk/P in Complex with B.Subtilis P-Ser-Hpr within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca403 b:45.1 occ:1.00 OE1 C:GLU204 2.7 47.4 1.0 O1P J:SEP46 2.8 57.0 0.8 O C:GLU204 2.8 41.5 1.0 O C:HOH543 2.8 34.3 1.0 OG C:SER162 3.0 41.9 1.0 O3 C:PO4503 3.4 44.7 0.8 CB C:SER162 3.4 37.8 1.0 CD C:GLU204 3.7 46.7 1.0 C C:GLU204 3.9 41.3 1.0 NH1 B:ARG245 3.9 61.6 1.0 P J:SEP46 4.0 59.5 0.8 OE2 C:GLU204 4.3 48.2 1.0 O3P J:SEP46 4.3 59.9 0.8 CB C:GLU204 4.3 41.3 1.0 O1 C:PO4503 4.4 47.0 0.8 P C:PO4503 4.4 43.9 0.8 OE1 C:GLU163 4.6 42.8 1.0 N C:SER162 4.6 33.5 1.0 CA C:SER162 4.6 33.9 1.0 CG C:GLU204 4.6 44.0 1.0 CA C:GLU204 4.6 40.4 1.0 OE2 C:GLU163 4.7 43.0 1.0 O4 C:PO4503 4.7 48.1 0.8 N C:ILE205 4.8 38.0 1.0 CA C:ILE205 4.9 39.3 1.0 N C:GLU204 4.9 39.3 1.0 OG J:SEP46 5.0 57.2 1.0 OD1 C:ASP178 5.0 43.8 1.0

S.Fieulaine, S.Morera, S.Poncet, I.Mijakovic, A.Galinier, J.Janin, J.Deutscher, S.Nessler. X-Ray Structure of A Bifunctional Protein Kinase in Complex with Its Protein Substrate Hpr. Proc.Natl.Acad.Sci.Usa V. 99 13437 2002.
ISSN: ISSN 0027-8424
PubMed: 12359875
DOI: 10.1073/PNAS.192368699