Chlorine in PDB 4fk9: High Resolution Structure of the Catalytic Domain of Mannanase SACTE_2347 From Streptomyces Sp. Sirexaa-E

The structure of High Resolution Structure of the Catalytic Domain of Mannanase SACTE_2347 From Streptomyces Sp. Sirexaa-E, PDB code: 4fk9 was solved by J.F.Acheson, T.E.Takasuka, B.G.Fox, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.77 / 1.06
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	62.805, 102.360, 45.346, 90.00, 90.00, 90.00
R / Rfree (%)	11.9 / 13.2

The structure of High Resolution Structure of the Catalytic Domain of Mannanase SACTE_2347 From Streptomyces Sp. Sirexaa-E also contains other interesting chemical elements:

Magnesium

(Mg)

5 atoms

The binding sites of Chlorine atom in the High Resolution Structure of the Catalytic Domain of Mannanase SACTE_2347 From Streptomyces Sp. Sirexaa-E (pdb code 4fk9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the High Resolution Structure of the Catalytic Domain of Mannanase SACTE_2347 From Streptomyces Sp. Sirexaa-E, PDB code: 4fk9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the High Resolution Structure of the Catalytic Domain of Mannanase SACTE_2347 From Streptomyces Sp. Sirexaa-E


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of High Resolution Structure of the Catalytic Domain of Mannanase SACTE_2347 From Streptomyces Sp. Sirexaa-E within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:44.8 occ:1.00 HG1 A:THR251 2.1 22.3 1.0 O A:HOH730 2.7 33.2 1.0 HE3 A:LYS254 2.8 23.8 1.0 O A:HOH874 2.9 34.5 1.0 OG1 A:THR251 2.9 18.6 1.0 HG21 A:THR251 3.0 22.8 1.0 HG3 A:LYS254 3.0 20.4 1.0 HB3 A:ALA253 3.2 21.8 1.0 CB A:THR251 3.7 17.9 1.0 HB A:THR251 3.7 21.5 1.0 CG2 A:THR251 3.7 19.0 1.0 CE A:LYS254 3.7 19.8 1.0 CG A:LYS254 3.9 17.0 1.0 HE2 A:LYS254 4.0 23.8 1.0 HG23 A:THR251 4.1 22.8 1.0 H A:LYS254 4.1 17.6 1.0 CB A:ALA253 4.1 18.2 1.0 CD A:LYS254 4.2 18.4 1.0 HG2 A:LYS254 4.3 20.4 1.0 HD2 A:LYS254 4.3 22.1 1.0 HB1 A:ALA253 4.5 21.8 1.0 HG22 A:THR251 4.5 22.8 1.0 HB2 A:ALA253 4.5 21.8 1.0 O A:HOH660 4.5 22.9 1.0 N A:LYS254 4.6 14.7 1.0 H A:ALA253 4.6 19.1 1.0 NZ A:LYS254 4.8 20.2 1.0 HZ1 A:LYS254 4.8 24.3 1.0 HZ3 A:LYS254 4.8 24.3 1.0

Chlorine binding site 2 out of 2 in the High Resolution Structure of the Catalytic Domain of Mannanase SACTE_2347 From Streptomyces Sp. Sirexaa-E


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of High Resolution Structure of the Catalytic Domain of Mannanase SACTE_2347 From Streptomyces Sp. Sirexaa-E within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl406 b:13.7 occ:1.00 H A:GLY83 2.3 10.7 1.0 HA A:TYR81 2.8 9.2 1.0 O A:HOH772 3.0 25.6 1.0 O A:HOH962 3.0 27.4 1.0 N A:GLY83 3.2 8.9 1.0 HD2 A:PRO82 3.2 11.3 1.0 HA3 A:GLY83 3.2 10.9 1.0 HD1 A:TYR81 3.2 11.5 1.0 HG2 A:GLU84 3.3 10.8 1.0 CA A:TYR81 3.5 7.7 1.0 C A:TYR81 3.6 7.5 1.0 CA A:GLY83 3.6 9.1 1.0 HB3 A:TYR81 3.7 9.6 1.0 N A:PRO82 3.7 8.5 1.0 HG2 A:PRO82 3.8 12.5 1.0 CD A:PRO82 3.8 9.4 1.0 CD1 A:TYR81 4.0 9.6 1.0 CB A:TYR81 4.1 8.0 1.0 O A:TYR81 4.1 7.8 1.0 C A:GLY83 4.2 8.3 1.0 CG A:GLU84 4.2 9.0 1.0 H A:GLU84 4.2 9.2 1.0 C A:PRO82 4.3 9.1 1.0 CG A:PRO82 4.3 10.4 1.0 N A:GLU84 4.4 7.6 1.0 HG3 A:GLU84 4.4 10.8 1.0 HA2 A:GLY83 4.5 10.9 1.0 CG A:TYR81 4.5 8.5 1.0 CA A:PRO82 4.5 9.3 1.0 O A:TRP80 4.6 9.8 1.0 HD3 A:PRO82 4.7 11.3 1.0 O A:HOH993 4.7 31.5 1.0 N A:TYR81 4.7 7.7 1.0 OE1 A:GLU84 4.8 12.4 1.0 O A:GLY83 5.0 10.0 1.0 HB2 A:TYR81 5.0 9.6 1.0 CD A:GLU84 5.0 10.6 1.0

T.E.Takasuka, J.F.Acheson, C.M.Bianchetti, B.M.Prom, L.F.Bergeman, A.J.Book, C.R.Currie, B.G.Fox. Biochemical Properties and Atomic Resolution Structure of A Proteolytically Processed Beta-Mannanase From Cellulolytic Streptomyces Sp. Sirexaa-E. Plos One V. 9 94166 2014.
ISSN: ESSN 1932-6203
PubMed: 24710170
DOI: 10.1371/JOURNAL.PONE.0094166