Nickel in PDB 1nm2: Malonyl-Coa:Acp Transacylase

All present enzymatic activity of Malonyl-Coa:Acp Transacylase:
2.3.1.39;

The structure of Malonyl-Coa:Acp Transacylase, PDB code: 1nm2 was solved by A.T.Keatinge-Clay, A.A.Shelat, D.F.Savage, S.Tsai, L.J.W.Miercke, J.D.O'connell Iii, C.Khosla, R.M.Stroud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.81 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.067, 54.486, 109.880, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 23.2

The binding sites of Nickel atom in the Malonyl-Coa:Acp Transacylase (pdb code 1nm2). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Malonyl-Coa:Acp Transacylase, PDB code: 1nm2:

Nickel binding site 1 out of 1 in the Malonyl-Coa:Acp Transacylase


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Malonyl-Coa:Acp Transacylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni317 b:28.9 occ:1.00 O A:HOH531 1.8 24.6 1.0 OD2 A:ASP51 2.1 23.9 1.0 OD2 A:ASP49 2.2 29.2 1.0 OD1 A:ASP49 2.7 26.4 1.0 CG A:ASP49 2.7 25.9 1.0 CG A:ASP51 3.0 20.1 1.0 OD1 A:ASP51 3.3 17.1 1.0 O A:HOH532 3.9 35.8 1.0 OE2 A:GLU52 4.1 28.6 1.0 CB A:ASP49 4.2 24.4 1.0 CB A:ASP51 4.4 20.4 1.0 CG A:GLU52 4.4 26.6 1.0 CD A:GLU52 4.7 28.3 1.0

A.T.Keatinge-Clay, A.A.Shelat, D.F.Savage, S.Tsai, L.J.W.Miercke, J.D.O'connell Iii, C.Khosla, R.M.Stroud. Catalysis, Specificity, and Acp Docking Site of Streptomyces Coelicolor Malonyl-Coa:Acp Transacylase Structure V. 11 147 2003.
ISSN: ISSN 0969-2126
PubMed: 12575934
DOI: 10.1016/S0969-2126(03)00004-2