Lead in PDB 1ocx: E. Coli Maltose-O-Acetyltransferase

All present enzymatic activity of E. Coli Maltose-O-Acetyltransferase:
2.3.1.79;

The structure of E. Coli Maltose-O-Acetyltransferase, PDB code: 1ocx was solved by L.Lo Leggio, F.Dal Degan, P.Poulsen, S.Larsen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.15
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	64.623, 106.238, 175.433, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 23.5

The binding sites of Lead atom in the E. Coli Maltose-O-Acetyltransferase (pdb code 1ocx). This binding sites where shown within 5.0 Angstroms radius around Lead atom.
In total 5 binding sites of Lead where determined in the E. Coli Maltose-O-Acetyltransferase, PDB code: 1ocx:
Jump to Lead binding site number: 1; 2; 3; 4; 5;

Lead binding site 1 out of 5 in the E. Coli Maltose-O-Acetyltransferase


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 1 of E. Coli Maltose-O-Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Pb1184 b:46.3 occ:0.50 PB A:PBM1184 0.0 46.3 0.5 C2 A:PBM1184 2.2 46.2 0.5 C1 A:PBM1184 2.2 46.4 0.5 C3 A:PBM1184 2.2 47.0 0.5 OE2 A:GLU6 2.8 69.3 1.0 OE1 A:GLU6 3.0 66.4 1.0 CD A:GLU6 3.3 67.5 1.0 CG A:GLU6 4.8 63.0 1.0 CG2 A:THR3 4.9 76.2 1.0

Lead binding site 2 out of 5 in the E. Coli Maltose-O-Acetyltransferase


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 2 of E. Coli Maltose-O-Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Pb1185 b:65.7 occ:0.40 PB A:PBM1185 0.0 65.7 0.4 C1 A:PBM1185 2.2 65.3 0.4 C3 A:PBM1185 2.2 65.8 0.4 C2 A:PBM1185 2.2 65.3 0.4 NE2 A:HIS113 2.4 55.6 1.0 CD2 A:HIS113 3.3 53.3 1.0 CE1 A:HIS113 3.4 57.1 1.0 OD1 C:ASN83 4.4 45.5 1.0 CG A:HIS113 4.5 53.4 1.0 ND1 A:HIS113 4.5 55.9 1.0 CB A:ALA111 4.9 47.6 1.0

Lead binding site 3 out of 5 in the E. Coli Maltose-O-Acetyltransferase


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 3 of E. Coli Maltose-O-Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Pb1184 b:46.5 occ:0.60 PB B:PBM1184 0.0 46.5 0.6 C3 B:PBM1184 2.2 46.5 0.6 C2 B:PBM1184 2.2 47.0 0.6 C1 B:PBM1184 2.2 47.4 0.6 OE2 B:GLU6 2.7 39.4 1.0 OE1 B:GLU6 2.8 36.9 1.0 CD B:GLU6 3.1 39.7 1.0 CG B:GLU6 4.6 40.0 1.0 N B:THR3 4.8 47.4 1.0 CA B:SER2 4.9 50.2 1.0

Lead binding site 4 out of 5 in the E. Coli Maltose-O-Acetyltransferase


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 4 of E. Coli Maltose-O-Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Pb1185 b:54.0 occ:0.40 PB B:PBM1185 0.0 54.0 0.4 C3 B:PBM1185 2.2 54.9 0.4 C1 B:PBM1185 2.2 55.6 0.4 C2 B:PBM1185 2.2 54.7 0.4 NE2 B:HIS113 2.3 46.2 1.0 CD2 B:HIS113 3.2 44.6 1.0 CE1 B:HIS113 3.2 45.9 1.0 O A:HOH2037 3.3 49.8 1.0 ND1 B:HIS113 4.3 43.9 1.0 CG B:HIS113 4.3 43.3 1.0 OD1 A:ASN83 4.5 38.2 1.0 O B:HOH2080 4.9 50.3 1.0 CB B:ALA111 4.9 33.8 1.0

Lead binding site 5 out of 5 in the E. Coli Maltose-O-Acetyltransferase


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 5 of E. Coli Maltose-O-Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ C:Pb1184 b:58.5 occ:0.40 PB C:PBM1184 0.0 58.5 0.4 C3 C:PBM1184 2.2 57.6 0.4 C2 C:PBM1184 2.2 57.8 0.4 C1 C:PBM1184 2.2 58.6 0.4 NE2 C:HIS113 2.3 34.9 1.0 CD2 C:HIS113 3.2 34.7 1.0 CE1 C:HIS113 3.3 36.4 1.0 ND1 C:HIS113 4.4 39.0 1.0 CG C:HIS113 4.4 35.8 1.0 OD1 B:ASN83 4.4 36.3 1.0 NE1 B:TRP137 4.8 34.9 1.0 CE1 B:PHE81 4.9 34.7 1.0 O C:HOH2017 4.9 54.7 1.0

L.Lo Leggio, F.D.Degan, P.Poulsen, S.M.Andersen, S.Larsen. The Structure and Specificity of Escherichia Coli Maltose Acetyltransferase Give New Insight Into the Laca Family of Acyltransferases. Biochemistry V. 42 5225 2003.
ISSN: ISSN 0006-2960
PubMed: 12731863
DOI: 10.1021/BI0271446