Chlorine in PDB 1diq: Crystal Structure of P-Cresol Methylhydroxylase with Substrate Bound

All present enzymatic activity of Crystal Structure of P-Cresol Methylhydroxylase with Substrate Bound:
1.17.99.1;

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

Resolution Low / High (Å)	25.00 / 2.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	139.100, 130.500, 74.400, 90.00, 90.00, 90.00
R / Rfree (%)	13.3 / 18.3

The structure of Crystal Structure of P-Cresol Methylhydroxylase with Substrate Bound also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of P-Cresol Methylhydroxylase with Substrate Bound (pdb code 1diq). 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 with Substrate Bound, PDB code: 1diq:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of P-Cresol Methylhydroxylase with Substrate Bound


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 with Substrate Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl702 b:39.2 occ:1.00 N A:GLY94 3.2 24.5 1.0 N A:GLY96 3.3 26.1 1.0 N A:MET48 3.4 28.8 1.0 OG A:SER97 3.4 29.5 1.0 N A:SER97 3.5 28.6 1.0 CA A:GLY96 3.8 27.6 1.0 C A:GLY96 3.8 29.3 1.0 CA A:GLY94 3.8 21.4 1.0 N A:TYR95 3.8 25.3 1.0 CB A:MET48 3.9 24.1 1.0 CB A:SER97 4.0 31.2 1.0 C A:GLY94 4.1 26.0 1.0 CA A:MET48 4.1 29.4 1.0 CG A:MET49 4.1 31.2 1.0 CG A:MET48 4.2 26.6 1.0 O A:ASN92 4.2 26.5 1.0 CA A:ILE47 4.2 31.4 1.0 C A:PHE93 4.2 27.0 1.0 C A:ILE47 4.3 29.6 1.0 CA A:PHE93 4.3 25.0 1.0 CA A:SER97 4.3 29.5 1.0 N A:MET49 4.4 28.1 1.0 C A:MET48 4.4 27.7 1.0 O A:GLY96 4.5 28.1 1.0 C A:TYR95 4.5 28.0 1.0 CB A:ILE47 4.5 31.3 1.0 CA A:TYR95 4.7 24.2 1.0 CG2 A:ILE47 4.8 29.5 1.0 O A:HOH848 4.8 44.0 1.0 O A:SER392 4.8 30.7 1.0 SD A:MET49 4.9 34.0 1.0 SD A:MET48 5.0 40.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of P-Cresol Methylhydroxylase with Substrate Bound


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 with Substrate Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl701 b:36.8 occ:1.00 N B:GLY94 3.3 24.4 1.0 N B:MET48 3.3 32.3 1.0 N B:GLY96 3.3 27.5 1.0 OG B:SER97 3.3 23.4 1.0 N B:SER97 3.5 31.5 1.0 CA B:GLY96 3.7 29.4 1.0 C B:GLY96 3.7 31.7 1.0 CA B:GLY94 3.9 23.6 1.0 N B:TYR95 3.9 25.2 1.0 CB B:MET48 4.0 31.1 1.0 CB B:SER97 4.0 31.4 1.0 CG B:MET49 4.1 29.9 1.0 CA B:MET48 4.1 33.6 1.0 C B:GLY94 4.1 28.1 1.0 CA B:ILE47 4.2 30.4 1.0 CG B:MET48 4.2 28.7 1.0 C B:ILE47 4.2 32.9 1.0 O B:ASN92 4.3 25.6 1.0 C B:PHE93 4.3 24.8 1.0 CA B:SER97 4.3 31.3 1.0 N B:MET49 4.3 32.1 1.0 CA B:PHE93 4.4 22.0 1.0 O B:GLY96 4.4 33.9 1.0 C B:MET48 4.4 32.2 1.0 CB B:ILE47 4.5 25.7 1.0 C B:TYR95 4.5 31.2 1.0 CG2 B:ILE47 4.7 20.5 1.0 CA B:TYR95 4.7 26.9 1.0 SD B:MET49 4.8 35.8 1.0 O B:SER392 4.9 30.0 1.0 CE B:MET49 5.0 26.1 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