Chlorine in PDB 1dii: Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution

All present enzymatic activity of Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution:
1.17.99.1;

The structure of Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution, PDB code: 1dii was solved by L.M.Cunane, Z.W.Chen, N.Shamala, F.S.Mathews, C.N.Cronin, W.S.Mcintire, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	140.300, 130.600, 74.100, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 23

The structure of Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution (pdb code 1dii). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution, PDB code: 1dii:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl701 b:29.3 occ:1.00 N A:GLY94 3.2 20.4 1.0 OG A:SER97 3.3 28.9 1.0 N A:GLY96 3.3 17.0 1.0 N A:MET48 3.3 22.9 1.0 N A:SER97 3.6 24.4 1.0 C A:GLY96 3.8 25.6 1.0 N A:TYR95 3.8 22.2 1.0 CA A:GLY94 3.8 20.1 1.0 CA A:GLY96 3.8 19.4 1.0 CB A:MET48 3.8 14.2 1.0 CG A:MET48 4.0 11.8 1.0 CA A:MET48 4.0 17.5 1.0 C A:GLY94 4.1 24.8 1.0 CB A:SER97 4.1 31.4 1.0 CG A:MET49 4.1 25.3 1.0 O A:ASN92 4.2 21.2 1.0 C A:PHE93 4.2 26.6 1.0 CA A:ILE47 4.3 21.5 1.0 C A:ILE47 4.3 24.8 1.0 CA A:PHE93 4.3 18.1 1.0 N A:MET49 4.4 28.7 1.0 C A:MET48 4.4 22.3 1.0 CA A:SER97 4.4 25.2 1.0 C A:TYR95 4.4 19.5 1.0 O A:GLY96 4.4 28.2 1.0 CB A:ILE47 4.6 21.2 1.0 CA A:TYR95 4.7 18.6 1.0 O A:SER392 4.7 27.9 1.0 O A:HOH742 4.8 36.2 1.0 SD A:MET48 4.9 27.6 1.0 CG2 A:ILE47 4.9 17.3 1.0 SD A:MET49 4.9 27.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of P-Cresol Methylhydroxylase at 2.5 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl702 b:31.8 occ:1.00 N B:GLY94 3.3 26.0 1.0 N B:GLY96 3.3 19.0 1.0 N B:MET48 3.4 21.8 1.0 OG B:SER97 3.4 23.8 1.0 N B:SER97 3.6 28.7 1.0 CA B:GLY96 3.7 26.1 1.0 C B:GLY96 3.8 27.9 1.0 N B:TYR95 3.8 19.5 1.0 CA B:GLY94 3.8 19.1 1.0 CB B:MET48 3.9 20.6 1.0 CA B:MET48 4.1 24.4 1.0 C B:GLY94 4.1 18.9 1.0 CG B:MET48 4.1 4.4 1.0 CG B:MET49 4.1 21.3 1.0 CB B:SER97 4.1 28.3 1.0 O B:ASN92 4.2 22.6 1.0 C B:PHE93 4.3 21.6 1.0 CA B:ILE47 4.3 22.9 1.0 C B:ILE47 4.3 22.8 1.0 N B:MET49 4.4 25.5 1.0 CA B:PHE93 4.4 16.3 1.0 CA B:SER97 4.4 23.9 1.0 C B:MET48 4.4 25.2 1.0 C B:TYR95 4.4 19.0 1.0 O B:GLY96 4.4 26.2 1.0 CB B:ILE47 4.6 23.9 1.0 CA B:TYR95 4.7 21.9 1.0 O B:SER392 4.8 30.7 1.0 CG2 B:ILE47 4.9 22.5 1.0 SD B:MET49 4.9 30.6 1.0 SD B:MET48 4.9 29.2 1.0 O B:GLY94 5.0 14.1 1.0

L.M.Cunane, Z.W.Chen, N.Shamala, F.S.Mathews, C.N.Cronin, W.S.Mcintire. Structures of the Flavocytochrome P-Cresol Methylhydroxylase and Its Enzyme-Substrate Complex: Gated Substrate Entry and Proton Relays Support the Proposed Catalytic Mechanism. J.Mol.Biol. V. 295 357 2000.
ISSN: ISSN 0022-2836
PubMed: 10623531
DOI: 10.1006/JMBI.1999.3290