Calcium in PDB 3ab9: Crystal Structure of Lipoylated E. Coli H-Protein (Reduced Form)

The structure of Crystal Structure of Lipoylated E. Coli H-Protein (Reduced Form), PDB code: 3ab9 was solved by K.Okamura-Ikeda, N.Maita, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.65
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	60.255, 60.255, 68.586, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 21.6

The structure of Crystal Structure of Lipoylated E. Coli H-Protein (Reduced Form) also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Calcium atom in the Crystal Structure of Lipoylated E. Coli H-Protein (Reduced Form) (pdb code 3ab9). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Lipoylated E. Coli H-Protein (Reduced Form), PDB code: 3ab9:

Calcium binding site 1 out of 1 in the Crystal Structure of Lipoylated E. Coli H-Protein (Reduced Form)


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 Lipoylated E. Coli H-Protein (Reduced Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca129 b:21.9 occ:1.00 O A:LEU44 2.2 20.4 1.0 OD1 A:ASP43 2.3 21.6 1.0 O A:HOH171 2.3 23.7 1.0 O A:HOH170 2.4 31.0 1.0 O A:HOH174 2.5 34.8 1.0 C A:LEU44 3.4 21.0 1.0 CG A:ASP43 3.5 21.1 1.0 N A:LEU44 3.7 19.2 1.0 OD2 A:ASP43 4.1 23.7 1.0 CA A:LEU44 4.1 20.5 1.0 C A:ASP43 4.2 20.7 1.0 N A:PRO45 4.5 21.8 1.0 CA A:ASP43 4.6 20.1 1.0 CB A:ASP43 4.6 20.7 1.0 CA A:PRO45 4.7 23.4 1.0 CB A:LEU44 4.8 18.9 1.0 C A:PRO45 4.8 23.7 1.0 O A:ASP43 4.9 21.2 1.0 O A:PRO45 4.9 23.7 1.0

K.Okamura-Ikeda, H.Hosaka, N.Maita, K.Fujiwara, A.C.Yoshizawa, A.Nakagawa, H.Taniguchi. Crystal Structure of Aminomethyltransferase in Complex with Dihydrolipoyl-H-Protein of the Glycine Cleavage System: Implications For Recognition of Lipoyl Protein Substrate, Disease-Related Mutations, and Reaction Mechanism J.Biol.Chem. V. 285 18684 2010.
ISSN: ISSN 0021-9258
PubMed: 20375021
DOI: 10.1074/JBC.M110.110718