Magnesium in PDB 4kjd: Ratintestinal Ap Expressed in E. Coli

All present enzymatic activity of Ratintestinal Ap Expressed in E. Coli:
3.1.3.1;

The structure of Ratintestinal Ap Expressed in E. Coli, PDB code: 4kjd was solved by K.Ghosh, R.K.Anumula, B.K.Laksmaiah, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.68 / 2.21
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.321, 75.726, 170.710, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 20.3

The binding sites of Magnesium atom in the Ratintestinal Ap Expressed in E. Coli (pdb code 4kjd). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Ratintestinal Ap Expressed in E. Coli, PDB code: 4kjd:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Ratintestinal Ap Expressed in E. Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ratintestinal Ap Expressed in E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:60.7 occ:1.00 O A:HOH735 2.0 60.6 1.0 OE2 A:GLU311 2.0 45.6 1.0 O A:HOH737 2.2 51.5 1.0 O A:HOH734 2.3 50.4 1.0 O A:HOH736 2.3 51.3 1.0 OG A:SER155 2.3 42.0 1.0 CD A:GLU311 3.0 54.4 1.0 CB A:SER155 3.4 32.4 1.0 OE1 A:GLU311 3.5 51.4 1.0 OD1 A:ASP42 3.8 71.3 1.0 ND1 A:HIS153 4.0 43.9 1.0 CB A:ASP42 4.0 48.0 1.0 CG A:ASP42 4.0 70.2 1.0 OD2 A:ASP357 4.3 63.1 1.0 CG A:GLU311 4.3 38.9 1.0 N A:SER155 4.4 31.6 1.0 O A:HOH649 4.4 36.1 1.0 CA A:SER155 4.5 31.2 1.0 O A:GLY313 4.6 47.4 1.0 OG A:SEP92 4.6 39.7 0.7 CB A:SEP92 4.6 37.2 1.0 CE1 A:HIS153 4.6 44.4 1.0 CA A:GLY313 4.6 42.6 1.0 O1P A:SEP92 4.7 42.4 1.0 OD2 A:ASP42 4.8 82.0 1.0 CD2 A:LEU40 4.9 37.7 1.0 CG2 A:THR149 4.9 36.4 1.0

Magnesium binding site 2 out of 4 in the Ratintestinal Ap Expressed in E. Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Ratintestinal Ap Expressed in E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:42.0 occ:1.00 O A:HOH634 2.2 41.0 1.0 OD1 A:ASP285 2.3 61.0 1.0 O A:PHE269 2.4 32.5 1.0 OE2 A:GLU270 2.4 56.8 1.0 OE1 A:GLU216 2.6 70.7 1.0 OE2 A:GLU216 3.2 69.2 1.0 CD A:GLU216 3.2 77.5 1.0 CD A:GLU270 3.5 68.0 1.0 CG A:ASP285 3.6 59.2 1.0 C A:PHE269 3.6 32.4 1.0 O A:HOH699 4.0 50.5 1.0 CG A:GLU270 4.1 45.8 1.0 OD2 A:ASP285 4.3 63.8 1.0 CA A:PHE269 4.4 27.7 1.0 CB A:PHE269 4.4 28.9 1.0 CB A:ASP285 4.5 43.5 1.0 O A:ALA284 4.6 44.5 1.0 O A:TRP248 4.6 34.5 1.0 OE1 A:GLU270 4.6 62.4 1.0 N A:GLU270 4.6 29.3 1.0 NH2 A:ARG204 4.7 32.2 1.0 CA A:GLU270 4.7 29.8 1.0 CG A:GLU216 4.7 54.1 1.0 NH1 A:ARG204 4.7 28.9 1.0 CA A:ASP285 4.8 40.0 1.0 OH A:TYR217 4.9 66.1 1.0 C A:ALA284 4.9 44.6 1.0 CB A:GLU270 5.0 31.6 1.0

Magnesium binding site 3 out of 4 in the Ratintestinal Ap Expressed in E. Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Ratintestinal Ap Expressed in E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:56.8 occ:1.00 OE2 B:GLU311 2.0 52.2 1.0 O B:HOH738 2.0 57.9 1.0 O B:HOH739 2.1 56.8 1.0 OG B:SER155 2.2 44.0 1.0 O B:HOH704 2.4 45.8 1.0 O B:HOH737 2.4 58.9 1.0 CD B:GLU311 3.0 58.2 1.0 CB B:SER155 3.2 34.6 1.0 OE1 B:GLU311 3.4 49.3 1.0 ND1 B:HIS153 4.0 44.3 1.0 N B:SER155 4.2 32.0 1.0 OD2 B:ASP357 4.2 58.8 1.0 OD1 B:ASP42 4.3 68.9 1.0 CG B:GLU311 4.3 40.0 1.0 CA B:SER155 4.3 31.6 1.0 O B:HOH697 4.4 37.3 1.0 CB B:ASP42 4.4 41.2 1.0 CG B:ASP42 4.5 65.0 1.0 CB B:SEP92 4.6 37.2 1.0 O B:HOH740 4.6 67.7 1.0 OG B:SEP92 4.6 38.1 1.0 CE1 B:HIS153 4.6 44.5 1.0 CA B:GLY313 4.7 40.4 1.0 O B:GLY313 4.7 47.0 1.0 O1P B:SEP92 4.8 36.9 1.0 CD B:PRO156 4.9 31.0 1.0 CG2 B:THR149 4.9 43.0 1.0 CD2 B:LEU40 5.0 41.1 1.0

Magnesium binding site 4 out of 4 in the Ratintestinal Ap Expressed in E. Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Ratintestinal Ap Expressed in E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:45.9 occ:1.00 O B:PHE269 2.4 30.8 1.0 O B:HOH609 2.4 37.8 1.0 OD1 B:ASP285 2.4 66.6 1.0 OE2 B:GLU270 2.5 54.3 1.0 OE1 B:GLU216 2.5 68.8 1.0 OE2 B:GLU216 3.2 77.2 1.0 CD B:GLU216 3.2 77.2 1.0 C B:PHE269 3.5 31.4 1.0 CD B:GLU270 3.6 65.6 1.0 CG B:ASP285 3.6 64.0 1.0 CG B:GLU270 4.0 45.1 1.0 NZ B:LYS275 4.1 82.8 1.0 O B:HOH719 4.2 46.0 1.0 CA B:PHE269 4.3 26.5 1.0 OD2 B:ASP285 4.3 71.4 1.0 CB B:PHE269 4.4 27.5 1.0 N B:GLU270 4.5 28.9 1.0 O B:TRP248 4.5 30.9 1.0 O B:ALA284 4.6 38.8 1.0 OH B:TYR217 4.6 52.1 1.0 CB B:ASP285 4.6 39.8 1.0 OE1 B:GLU270 4.6 66.6 1.0 CA B:GLU270 4.6 28.3 1.0 NH1 B:ARG204 4.7 19.9 1.0 NH2 B:ARG204 4.7 26.4 1.0 CG B:GLU216 4.7 49.0 1.0 CA B:ASP285 4.9 36.5 1.0 CB B:GLU270 4.9 30.0 1.0

K.Ghosh, D.Mazumder Tagore, R.Anumula, B.Lakshmaiah, P.P.Kumar, S.Singaram, T.Matan, S.Kallipatti, S.Selvam, P.Krishnamurthy, M.Ramarao. Crystal Structure of Rat Intestinal Alkaline Phosphatase - Role of Crown Domain in Mammalian Alkaline Phosphatases. J.Struct.Biol. V. 184 182 2013.
ISSN: ISSN 1047-8477
PubMed: 24076154
DOI: 10.1016/J.JSB.2013.09.017