Manganese in PDB 3ckn: Crystal Structure of A Mycobacterial Protein

The structure of Crystal Structure of A Mycobacterial Protein, PDB code: 3ckn was solved by Z.Marland, J.Rossjohn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.20
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	86.862, 86.862, 104.243, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 23.2

The binding sites of Manganese atom in the Crystal Structure of A Mycobacterial Protein (pdb code 3ckn). 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 A Mycobacterial Protein, PDB code: 3ckn:

Manganese binding site 1 out of 1 in the Crystal Structure of A Mycobacterial Protein


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 A Mycobacterial Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn330 b:60.8 occ:1.00 O A:HOH368 1.8 44.2 1.0 O A:HOH367 2.1 50.4 1.0 OD2 A:ASP141 2.2 38.3 1.0 O2B A:UDP332 2.2 70.1 1.0 O1A A:UDP332 2.3 63.5 1.0 ND1 A:HIS263 2.7 42.1 1.0 CG A:ASP141 2.9 36.5 1.0 OD1 A:ASP141 3.0 37.3 1.0 CE1 A:HIS263 3.2 42.5 1.0 PB A:UDP332 3.4 69.5 1.0 PA A:UDP332 3.5 62.7 1.0 O3A A:UDP332 3.8 65.9 1.0 CG A:HIS263 3.9 41.8 1.0 O1B A:UDP332 4.2 69.6 1.0 OD2 A:ASP139 4.2 32.7 1.0 C5' A:UDP332 4.3 57.1 1.0 CB A:ASP141 4.4 35.8 1.0 O5' A:UDP332 4.4 60.2 1.0 O A:ARG264 4.4 40.9 1.0 NE2 A:HIS263 4.5 43.0 1.0 CB A:HIS263 4.5 41.8 1.0 O3B A:UDP332 4.5 69.8 1.0 O2A A:UDP332 4.6 61.5 1.0 CD2 A:HIS263 4.8 42.3 1.0 NH2 A:ARG261 4.9 47.4 1.0 CG A:ASP139 4.9 33.1 1.0 CB A:ASP139 4.9 32.5 1.0 C3' A:UDP332 5.0 55.0 1.0

Z.Fulton, A.Mcalister, M.C.Wilce, R.Brammananth, L.Zaker-Tabrizi, M.A.Perugini, S.P.Bottomley, R.L.Coppel, P.K.Crellin, J.Rossjohn, T.Beddoe. Crystal Structure of A Udp-Glucose-Specific Glycosyltransferase From A Mycobacterium Species. J.Biol.Chem. V. 283 27881 2008.
ISSN: ISSN 0021-9258
PubMed: 18667419
DOI: 10.1074/JBC.M801853200