Lead in PDB 2fp1: Secreted Chorismate Mutase From Mycobacterium Tuberculosis

All present enzymatic activity of Secreted Chorismate Mutase From Mycobacterium Tuberculosis:
5.4.99.5;

The structure of Secreted Chorismate Mutase From Mycobacterium Tuberculosis, PDB code: 2fp1 was solved by M.Okvist, R.Dey, S.Sasso, E.Grahn, P.Kast, U.Krengel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.01 / 1.55
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.644, 72.673, 62.060, 90.00, 104.52, 90.00
R / Rfree (%)	17.4 / 21.1

The binding sites of Lead atom in the Secreted Chorismate Mutase From Mycobacterium Tuberculosis (pdb code 2fp1). This binding sites where shown within 5.0 Angstroms radius around Lead atom.
In total 2 binding sites of Lead where determined in the Secreted Chorismate Mutase From Mycobacterium Tuberculosis, PDB code: 2fp1:
Jump to Lead binding site number: 1; 2;

Lead binding site 1 out of 2 in the Secreted Chorismate Mutase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 1 of Secreted Chorismate Mutase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Pb501 b:12.5 occ:0.75 NE2 B:HIS151 2.5 9.3 1.0 OE2 B:GLU41 2.5 15.8 1.0 OE1 B:GLU41 2.7 18.2 1.0 O B:GLN38 2.8 14.4 1.0 O B:HOH564 2.8 21.5 1.0 CD B:GLU41 2.9 17.7 1.0 OE1 B:GLN38 3.0 33.4 1.0 O B:HOH540 3.1 22.8 1.0 CD2 B:HIS151 3.4 8.8 1.0 CE1 B:HIS151 3.5 11.5 1.0 C B:GLN38 3.6 15.1 1.0 CA B:GLN38 3.9 16.6 1.0 CD B:GLN38 4.2 26.4 1.0 CB B:GLN38 4.3 17.8 1.0 O B:HOH512 4.4 18.1 1.0 CG B:GLU41 4.4 15.6 1.0 O B:HOH604 4.5 41.7 1.0 CG B:HIS151 4.6 11.2 1.0 ND1 B:HIS151 4.6 10.8 1.0 O B:HOH552 4.7 26.7 1.0 O B:HOH537 4.8 25.9 1.0 N B:LEU39 4.8 14.0 1.0 CG B:GLN38 4.9 20.6 1.0

Lead binding site 2 out of 2 in the Secreted Chorismate Mutase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 2 of Secreted Chorismate Mutase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ B:Pb502 b:21.1 occ:0.25 OE1 B:GLU48 2.5 32.8 1.0 OE2 B:GLU48 2.6 33.0 1.0 OE2 B:GLU51 2.7 38.0 1.0 OE1 B:GLU51 2.8 36.6 1.0 CD B:GLU48 2.9 28.0 1.0 CD B:GLU51 3.2 33.7 1.0 CG B:GLU48 4.4 22.0 1.0 NH2 B:ARG175 4.6 28.2 1.0 O B:HOH607 4.7 39.1 1.0 CG B:GLU51 4.7 27.6 1.0 NH1 B:ARG175 4.7 32.6 1.0 O B:HOH652 4.9 38.1 1.0

M.Okvist, R.Dey, S.Sasso, E.Grahn, P.Kast, U.Krengel. 1.6A Crystal Structure of the Secreted Chorismate Mutase From Mycobacterium Tuberculosis: Novel Fold Topology Revealed J.Mol.Biol. V. 357 1483 2006.
ISSN: ISSN 0022-2836
PubMed: 16499927
DOI: 10.1016/J.JMB.2006.01.069