Manganese in PDB 2pml: Crystal Structure of PFPK7 in Complex with An Atp Analogue

The structure of Crystal Structure of PFPK7 in Complex with An Atp Analogue, PDB code: 2pml was solved by A.Merckx, A.Echalier, M.Noble, J.Endicott, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	72.554, 81.795, 138.273, 90.00, 90.00, 90.00
R / Rfree (%)	25.8 / 32.7

The binding sites of Manganese atom in the Crystal Structure of PFPK7 in Complex with An Atp Analogue (pdb code 2pml). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of PFPK7 in Complex with An Atp Analogue, PDB code: 2pml:

Manganese binding site 1 out of 1 in the Crystal Structure of PFPK7 in Complex with An Atp Analogue


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of PFPK7 in Complex with An Atp Analogue within 5.0Å range: probe atom residue distance (Å) B Occ X:Mn383 b:82.5 occ:1.00 O3G X:ANP381 1.7 84.6 1.0 O2A X:ANP381 2.3 72.7 1.0 OD2 X:ASP190 2.4 42.0 1.0 OD1 X:ASN177 2.5 41.8 1.0 O2B X:ANP381 2.9 79.1 1.0 PG X:ANP381 3.2 84.1 1.0 CG X:ASP190 3.2 38.4 1.0 CB X:ASP190 3.3 37.1 1.0 CG X:ASN177 3.4 40.1 1.0 ND2 X:ASN177 3.6 40.3 1.0 PA X:ANP381 3.7 71.7 1.0 NZ X:LYS174 3.7 44.2 1.0 N3B X:ANP381 3.8 81.0 1.0 PB X:ANP381 3.8 79.0 1.0 O2G X:ANP381 4.1 83.6 1.0 O1G X:ANP381 4.1 83.6 1.0 O3A X:ANP381 4.3 75.6 1.0 OG X:SER176 4.4 38.5 1.0 OD1 X:ASP190 4.4 40.3 1.0 O X:HOH401 4.5 42.8 1.0 O1A X:ANP381 4.5 72.4 1.0 O5' X:ANP381 4.7 70.2 1.0 CB X:ASN177 4.8 38.8 1.0 CA X:ASP190 4.9 37.1 1.0 C5' X:ANP381 4.9 67.0 1.0

A.Merckx, A.Echalier, K.Langford, A.Sicard, G.Langsley, J.Joore, C.Doerig, M.Noble, J.Endicott. Structures of PFPK7 An Atypical Protein Kinase From P. Falciparum Identify A Novel Activation Motif and Leads For Inhibitor Design To Be Published.