Mercury in PDB 1hdk: Charcot-Leyden Crystal Protein - Pcmbs Complex

All present enzymatic activity of Charcot-Leyden Crystal Protein - Pcmbs Complex:
3.1.1.5;

The structure of Charcot-Leyden Crystal Protein - Pcmbs Complex, PDB code: 1hdk was solved by S.J.Ackerman, M.P.Savage, L.Liu, D.D.Leonidas, M.A.Kwatia, G.J.Swaminathan, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.80
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	49.547, 49.547, 261.645, 90.00, 90.00, 120.00
R / Rfree (%)	19.9 / 22.1

The binding sites of Mercury atom in the Charcot-Leyden Crystal Protein - Pcmbs Complex (pdb code 1hdk). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Charcot-Leyden Crystal Protein - Pcmbs Complex, PDB code: 1hdk:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Charcot-Leyden Crystal Protein - Pcmbs Complex


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Charcot-Leyden Crystal Protein - Pcmbs Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg929 b:56.9 occ:1.00 HG A:PMB929 0.0 56.9 1.0 C4 A:PMB929 1.9 59.9 0.7 SG A:CYS29 2.6 36.4 1.0 C5 A:PMB929 2.8 60.3 0.7 C3 A:PMB929 2.8 59.4 0.7 CB A:CYS29 3.3 23.2 1.0 OD2 A:ASP85 3.4 31.7 1.0 OD1 A:ASP85 3.5 26.1 1.0 CA A:CYS29 3.6 19.5 1.0 CG A:ASP85 3.7 28.3 1.0 C6 A:PMB929 4.1 61.0 0.7 C2 A:PMB929 4.1 60.7 0.7 N A:PHE30 4.3 16.6 1.0 C A:CYS29 4.5 16.4 1.0 C1 A:PMB929 4.6 61.5 0.7 N A:CYS29 4.8 18.9 1.0

Mercury binding site 2 out of 2 in the Charcot-Leyden Crystal Protein - Pcmbs Complex


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Charcot-Leyden Crystal Protein - Pcmbs Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg957 b:33.7 occ:1.00 HG A:PMB957 0.0 33.7 1.0 C4 A:PMB957 1.9 41.6 0.7 SG A:CYS57 2.5 20.4 1.0 C3 A:PMB957 2.8 41.9 0.7 C5 A:PMB957 2.8 41.3 0.7 CB A:CYS57 3.3 16.9 1.0 OH A:TYR35 3.6 37.5 1.0 OE1 A:GLU33 3.6 26.2 1.0 NE A:ARG60 3.9 43.5 1.0 CD A:GLU33 4.1 24.6 1.0 CB A:ARG60 4.1 23.5 1.0 C2 A:PMB957 4.1 43.5 0.7 CZ A:TYR35 4.1 32.2 1.0 C6 A:PMB957 4.1 43.8 0.7 CG A:ARG60 4.2 31.4 1.0 CZ A:ARG60 4.3 45.6 1.0 NH1 A:ARG61 4.3 37.5 1.0 CD A:ARG60 4.4 37.4 1.0 NH2 A:ARG60 4.4 47.1 1.0 CE1 A:TYR35 4.5 28.1 1.0 C1 A:PMB957 4.7 44.2 0.7 OE2 A:GLU33 4.7 28.0 1.0 CG A:GLU33 4.7 22.1 1.0 CA A:CYS57 4.7 13.9 1.0 CD A:ARG61 4.9 27.6 1.0 CB A:GLU33 4.9 17.3 1.0 CE2 A:TYR35 4.9 31.1 1.0 CG A:ARG61 4.9 24.5 1.0 CZ A:ARG61 4.9 35.4 1.0 NH1 A:ARG60 5.0 46.7 1.0

S.J.Ackerman, L.Liu, M.A.Kwatia, M.P.Savage, D.D.Leonidas, G.J.Swaminathan, K.R.Acharya. Charcot-Leyden Crystal Protein (Galectin-10) Is Not A Dual Function Galectin with Lysophospholipase Activity But Binds A Lysophospholipase Inhibitor in A Novel Structural Fashion. J.Biol.Chem. V. 277 14859 2002.
ISSN: ISSN 0021-9258
PubMed: 11834744
DOI: 10.1074/JBC.M200221200