Calcium in PDB 2xec: Nocardia Farcinica Maleate Cis-Trans Isomerase Bound to Tris

All present enzymatic activity of Nocardia Farcinica Maleate Cis-Trans Isomerase Bound to Tris:
5.2.1.1;

The structure of Nocardia Farcinica Maleate Cis-Trans Isomerase Bound to Tris, PDB code: 2xec was solved by F.Fisch, C.Martinez-Fleites, N.Baudendistel, B.Hauer, J.P.Turkenburg, S.Hart, N.C.Bruce, G.Grogan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.67 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.160, 84.510, 238.130, 90.00, 90.00, 90.00
R / Rfree (%)	23.859 / 28.841

The binding sites of Calcium atom in the Nocardia Farcinica Maleate Cis-Trans Isomerase Bound to Tris (pdb code 2xec). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Nocardia Farcinica Maleate Cis-Trans Isomerase Bound to Tris, PDB code: 2xec:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Nocardia Farcinica Maleate Cis-Trans Isomerase Bound to Tris


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Nocardia Farcinica Maleate Cis-Trans Isomerase Bound to Tris within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1246 b:60.8 occ:1.00 O C:HOH2011 2.6 17.8 1.0 O C:HOH2009 3.2 11.7 1.0 OE1 B:GLU148 3.4 45.0 1.0 OE1 C:GLU148 3.5 53.0 1.0 NH1 B:ARG120 3.9 50.0 1.0 NH2 B:ARG120 3.9 49.1 1.0 NE2 C:HIS89 4.1 50.8 1.0 NH1 C:ARG120 4.3 42.7 1.0 CZ B:ARG120 4.4 51.5 1.0 CD B:GLU148 4.4 40.9 1.0 NE2 B:HIS89 4.5 34.8 1.0 CE1 C:HIS89 4.6 52.6 1.0 CD C:GLU148 4.7 53.3 1.0 OE2 B:GLU148 4.7 38.9 1.0 CG1 C:VAL116 4.8 41.2 1.0

Calcium binding site 2 out of 2 in the Nocardia Farcinica Maleate Cis-Trans Isomerase Bound to Tris


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Nocardia Farcinica Maleate Cis-Trans Isomerase Bound to Tris within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca1247 b:54.8 occ:1.00 O D:HOH2008 2.5 20.3 1.0 O A:HOH2023 2.6 25.1 1.0 O D:HOH2007 2.7 17.9 1.0 OE1 A:GLU148 2.7 51.4 1.0 OE1 D:GLU148 2.8 54.1 1.0 O A:HOH2027 2.8 9.8 1.0 CD D:GLU148 3.5 51.3 1.0 OE2 D:GLU148 3.6 53.4 1.0 CD A:GLU148 3.7 45.9 1.0 OE2 A:GLU148 4.0 45.5 1.0 NH2 A:ARG120 4.1 50.7 1.0 NE2 D:HIS89 4.1 50.1 1.0 NH1 D:ARG120 4.2 58.5 1.0 NH2 D:ARG120 4.3 56.1 1.0 NE2 A:HIS89 4.3 48.4 1.0 NH1 A:ARG120 4.4 53.5 1.0 CZ A:ARG120 4.7 53.2 1.0 CZ D:ARG120 4.8 57.5 1.0 CG D:GLU148 4.8 49.9 1.0 CA D:GLU148 4.9 53.3 1.0 CE1 D:HIS89 4.9 51.2 1.0 CD2 D:HIS89 4.9 51.2 1.0

F.Fisch, C.M.Fleites, M.Delenne, N.Baudendistel, B.Hauer, J.P.Turkenburg, S.Hart, N.C.Bruce, G.Grogan. A Covalent Succinylcysteine-Like Intermediate in the Enzyme-Catalyzed Transformation of Maleate to Fumarate By Maleate Isomerase. J.Am.Chem.Soc. V. 132 11455 2010.
ISSN: ISSN 0002-7863
PubMed: 20677745
DOI: 10.1021/JA1053576