Chlorine in PDB 1sd0: Structure of Arginine Kinase C271A Mutant

All present enzymatic activity of Structure of Arginine Kinase C271A Mutant:
2.7.3.3;

The structure of Structure of Arginine Kinase C271A Mutant, PDB code: 1sd0 was solved by J.L.Gattis, E.Ruben, M.O.Fenley, W.R.Ellington, M.S.Chapman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.905, 71.255, 79.980, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 23.6

The structure of Structure of Arginine Kinase C271A Mutant also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Chlorine atom in the Structure of Arginine Kinase C271A Mutant (pdb code 1sd0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of Arginine Kinase C271A Mutant, PDB code: 1sd0:

Chlorine binding site 1 out of 1 in the Structure of Arginine Kinase C271A Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Arginine Kinase C271A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:14.3 occ:1.00 OG1 A:THR273 2.8 23.5 1.0 CG2 A:THR273 3.2 29.5 1.0 N A:THR273 3.3 15.4 1.0 CB A:THR273 3.4 18.4 1.0 NH1 A:ARG403 3.4 11.8 1.0 O A:HOH467 3.4 31.0 1.0 CD A:PRO272 3.5 19.2 1.0 CB A:ALA271 3.5 28.9 1.0 CG A:PRO272 3.6 21.7 1.0 CG A:ARG403 3.6 22.6 1.0 CD A:ARG403 3.8 29.5 1.0 CG1 A:VAL65 3.9 19.1 1.0 N A:PRO272 3.9 22.8 1.0 CA A:THR273 4.0 23.7 1.0 CG2 A:VAL65 4.1 23.0 1.0 CB A:VAL65 4.1 30.5 1.0 C A:ALA271 4.3 23.9 1.0 C A:PRO272 4.3 24.4 1.0 CA A:ALA271 4.4 24.4 1.0 O A:ILE67 4.4 35.6 1.0 CZ A:ARG403 4.5 27.9 1.0 CA A:PRO272 4.5 18.9 1.0 NE A:ARG403 4.6 19.8 1.0 CB A:PRO272 4.7 19.8 1.0

J.L.Gattis, E.Ruben, M.O.Fenley, W.R.Ellington, M.S.Chapman. The Active Site Cysteine of Arginine Kinase: Structural and Functional Analysis of Partially Active Mutants Biochemistry V. 43 8680 2004.
ISSN: ISSN 0006-2960
PubMed: 15236576
DOI: 10.1021/BI049793I