Lead in PDB 4tkx: Structure of Protease

All present enzymatic activity of Structure of Protease:
3.4.22.47;

The structure of Structure of Protease, PDB code: 4tkx was solved by M.A.Gorman, M.W.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.71 / 1.60
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	116.941, 116.941, 86.852, 90.00, 90.00, 90.00
R / Rfree (%)	12 / 14.5

The structure of Structure of Protease also contains other interesting chemical elements:

Potassium	(K)	1 atom
Sodium	(Na)	2 atoms

The binding sites of Lead atom in the Structure of Protease (pdb code 4tkx). This binding sites where shown within 5.0 Angstroms radius around Lead atom.
In total only one binding site of Lead was determined in the Structure of Protease, PDB code: 4tkx:

Lead binding site 1 out of 1 in the Structure of Protease


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 1 of Structure of Protease within 5.0Å range: probe atom residue distance (Å) B Occ L:Pb719 b:11.8 occ:0.85 O L:HOH1238 2.5 19.5 1.0 OE2 L:GLU491 2.5 10.4 1.0 OD1 L:ASP313 2.5 11.5 1.0 O L:PHE482 2.6 10.3 1.0 OD2 L:ASP313 2.6 12.5 1.0 O L:HOH1275 2.6 22.6 1.0 O L:HOH1203 2.6 15.1 1.0 OE1 L:GLU491 2.7 13.1 1.0 CG L:ASP313 2.9 12.1 1.0 CD L:GLU491 2.9 10.4 1.0 C L:PHE482 3.5 10.3 1.0 HA L:PRO487 3.7 12.1 1.0 HB2 L:PHE482 3.8 11.9 1.0 HH22 L:ARG495 3.8 11.0 1.0 HA L:PHE482 3.9 10.9 1.0 O L:HOH1276 3.9 33.3 1.0 HA L:ASP483 3.9 14.3 1.0 HG L:SER350 4.0 11.1 1.0 HG1 L:THR314 4.1 16.3 1.0 CA L:PHE482 4.2 9.1 1.0 H L:THR314 4.2 10.7 1.0 H L:CYS488 4.3 11.1 1.0 NH2 L:ARG495 4.3 9.2 1.0 O L:HOH945 4.4 15.0 1.0 CG L:GLU491 4.5 8.5 1.0 HG23 L:THR314 4.5 16.9 1.0 CB L:ASP313 4.5 10.7 1.0 CB L:PHE482 4.5 9.9 1.0 N L:ASP483 4.5 10.5 1.0 O L:TYR484 4.5 13.6 1.0 HH21 L:ARG495 4.6 11.0 1.0 O L:HOH1082 4.6 20.2 1.0 CA L:ASP483 4.6 11.9 1.0 OG L:SER350 4.6 9.3 1.0 CA L:PRO487 4.7 10.1 1.0 H L:TYR484 4.7 15.2 1.0 O L:HOH1184 4.8 32.2 1.0 HG2 L:GLU491 4.8 10.2 1.0 OG1 L:THR314 4.8 13.6 1.0 HD1 L:PHE482 4.8 13.3 1.0 HB2 L:ASP313 4.8 12.8 1.0 HH12 L:ARG495 4.8 11.4 1.0 HB3 L:ASP313 4.9 12.8 1.0 HG3 L:GLU491 4.9 10.2 1.0 HA L:ASP313 5.0 9.7 1.0 O L:GLN486 5.0 12.8 0.4

M.A.Gorman, C.A.Seers, B.J.Michell, S.C.Feil, N.L.Huq, K.J.Cross, E.C.Reynolds, M.W.Parker. Structure of the Lysine Specific Protease Kgp From Porphyromonas Gingivalis, A Target For Improved Oral Health. Protein Sci. V. 24 162 2015.
ISSN: ESSN 1469-896X
PubMed: 25327141
DOI: 10.1002/PRO.2589