Chlorine in PDB 2c2n: Structure of Human Mitochondrial Malonyltransferase

The structure of Structure of Human Mitochondrial Malonyltransferase, PDB code: 2c2n was solved by X.Wu, G.Bunkoczi, C.Smee, C.Arrowsmith, M.Sundstrom, J.Weigelt, A.Edwards, F.Von Delft, U.Oppermann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.33 / 1.55
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.573, 84.828, 74.565, 90.00, 93.43, 90.00
R / Rfree (%)	17.8 / 21.8

The binding sites of Chlorine atom in the Structure of Human Mitochondrial Malonyltransferase (pdb code 2c2n). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of Human Mitochondrial Malonyltransferase, PDB code: 2c2n:

Chlorine binding site 1 out of 1 in the Structure of Human Mitochondrial Malonyltransferase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Human Mitochondrial Malonyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1342 b:13.3 occ:1.00 O B:HOH2007 3.0 25.4 1.0 O B:HOH2002 3.0 10.6 1.0 O B:HOH2064 3.1 14.9 1.0 O B:HOH2010 3.1 29.9 1.0 ND2 B:ASN193 3.4 14.3 1.0 CD2 B:HIS234 3.7 12.9 1.0 CE B:MET157 3.9 14.5 1.0 CE2 B:PHE116 3.9 11.7 1.0 CG B:ASN193 4.2 10.9 1.0 OD1 B:ASN193 4.3 12.9 1.0 NE2 B:HIS234 4.3 13.1 1.0 CB B:SER117 4.4 8.6 1.0 CB B:PHE233 4.4 10.0 1.0 OG B:SER117 4.5 9.3 1.0 CD2 B:PHE233 4.5 13.5 1.0 SD B:MET157 4.5 11.5 1.0 CD2 B:PHE116 4.8 7.4 1.0 CZ B:PHE116 4.8 10.2 1.0 CG B:HIS234 4.9 10.0 1.0 CG B:PHE233 5.0 10.1 1.0 O B:HOH2003 5.0 8.2 1.0

G.Bunkoczi, S.Misquitta, X.Wu, W.H.Lee, A.Rojkova, G.Kochan, K.L.Kavanagh, U.Oppermann, S.Smith. Structural Basis For Different Specificities of Acyltransferases Associated with the Human Cytosolic and Mitochondrial Fatty Acid Synthases. Chem.Biol. V. 16 667 2009.
ISSN: ISSN 1074-5521
PubMed: 19549604
DOI: 10.1016/J.CHEMBIOL.2009.04.011