Calcium in PDB 4onu: Camp-Binding Acyltransferase From Mycobacterium Smegmatis, E234A Mutant

The structure of Camp-Binding Acyltransferase From Mycobacterium Smegmatis, E234A Mutant, PDB code: 4onu was solved by M.Podobnik, K.Rebolj, S.S.Visweswariah, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	38.318, 82.764, 105.969, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 26.3

The binding sites of Calcium atom in the Camp-Binding Acyltransferase From Mycobacterium Smegmatis, E234A Mutant (pdb code 4onu). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Camp-Binding Acyltransferase From Mycobacterium Smegmatis, E234A Mutant, PDB code: 4onu:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Camp-Binding Acyltransferase From Mycobacterium Smegmatis, E234A Mutant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Camp-Binding Acyltransferase From Mycobacterium Smegmatis, E234A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:33.2 occ:1.00 N A:ARG186 3.1 30.6 1.0 O A:HOH520 3.2 20.6 1.0 CD A:ARG186 3.4 42.0 1.0 NH1 A:ARG186 3.5 39.4 1.0 CB A:ASP92 3.6 30.7 1.0 CB A:ARG186 3.7 32.4 1.0 CA A:ARG186 4.0 32.9 1.0 CG A:ARG186 4.0 40.2 1.0 OD2 A:ASP92 4.0 34.0 1.0 C A:VAL185 4.1 33.0 1.0 NE A:ARG186 4.1 41.9 1.0 NH1 A:ARG112 4.1 26.8 1.0 CA A:VAL185 4.2 30.7 1.0 CZ A:ARG186 4.2 40.6 1.0 CG A:ASP92 4.2 32.0 1.0 O A:SER184 4.3 46.5 1.0 O A:ARG186 4.7 27.3 1.0 CG1 A:VAL185 4.8 31.2 1.0 C A:ARG186 4.9 29.7 1.0 O A:ARG91 4.9 33.1 1.0 CA A:ASP92 4.9 31.1 1.0 O A:HOH614 5.0 42.3 1.0

Calcium binding site 2 out of 2 in the Camp-Binding Acyltransferase From Mycobacterium Smegmatis, E234A Mutant


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Camp-Binding Acyltransferase From Mycobacterium Smegmatis, E234A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca402 b:81.0 occ:1.00 O A:HOH538 2.6 47.5 1.0 CD1 A:LEU159 4.1 33.4 1.0 CD2 A:LEU214 4.2 62.8 1.0 CG2 A:ILE140 4.3 41.8 1.0 CB A:ALA137 4.3 36.1 1.0 CD A:PRO142 4.5 38.5 1.0 O A:ALA137 4.5 43.0 1.0 CD A:ARG156 4.5 37.9 1.0 O A:ILE140 4.5 45.6 1.0 CG A:PRO142 4.6 38.8 1.0 CA A:ALA137 4.6 40.0 1.0 CB A:ILE140 4.7 40.5 1.0 NE A:ARG156 4.7 36.2 1.0 O A:HOH579 4.9 55.9 1.0

M.Podobnik, N.Siddiqui, K.Rebolj, S.Nambi, F.Merzel, S.S.Visweswariah. Allostery and Conformational Dynamics in Camp-Binding Acyltransferases. J.Biol.Chem. V. 289 16588 2014.
ISSN: ISSN 0021-9258
PubMed: 24748621
DOI: 10.1074/JBC.M114.560086