Chlorine in PDB 2x6t: Agme Bound to Adp-B-Mannose

All present enzymatic activity of Agme Bound to Adp-B-Mannose:
5.1.3.20;

The structure of Agme Bound to Adp-B-Mannose, PDB code: 2x6t was solved by T.Kowatz, J.P.Morrison, M.E.Tanner, J.H.Naismith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.69 / 2.36
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	341.993, 60.787, 191.789, 90.00, 91.41, 90.00
R / Rfree (%)	18.932 / 20.889

The binding sites of Chlorine atom in the Agme Bound to Adp-B-Mannose (pdb code 2x6t). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Agme Bound to Adp-B-Mannose, PDB code: 2x6t:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Agme Bound to Adp-B-Mannose


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Agme Bound to Adp-B-Mannose within 5.0Å range: probe atom residue distance (Å) B Occ G:Cl1312 b:61.0 occ:1.00 NH2 G:ARG308 3.4 39.4 1.0 NH1 G:ARG308 3.5 38.5 1.0 NE1 G:TRP305 3.9 28.7 1.0 CZ G:ARG308 3.9 38.2 1.0 CD1 G:TRP305 4.3 28.9 1.0 NZ G:LYS17 4.9 32.0 1.0

Chlorine binding site 2 out of 2 in the Agme Bound to Adp-B-Mannose


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Agme Bound to Adp-B-Mannose within 5.0Å range: probe atom residue distance (Å) B Occ G:Cl1313 b:65.1 occ:1.00 NE G:ARG284 3.6 29.3 1.0 O G:HOH2129 4.0 41.3 1.0 NH2 G:ARG284 4.0 29.3 1.0 CD1 G:LEU280 4.1 27.9 1.0 CG G:ARG284 4.2 29.1 1.0 CZ G:ARG284 4.3 29.0 1.0 CB G:LEU280 4.3 28.5 1.0 O G:HOH2155 4.5 30.1 1.0 CD G:ARG284 4.5 29.4 1.0 CG G:LEU280 4.8 28.6 1.0

T.Kowatz, J.P.Morrison, M.E.Tanner, J.H.Naismith. The Crystal Structure of the Y140F Mutant of Adp-L- Glycero-D-Manno-Heptose 6-Epimerase Bound to Adp- Beta-D-Mannose Suggests A One Base Mechanism. Protein Sci. V. 19 1337 2010.
ISSN: ISSN 0961-8368
PubMed: 20506248
DOI: 10.1002/PRO.410