Chlorine in PDB 3mvt: Crystal Structure of Apo Mada at 2.2A Resolution

All present enzymatic activity of Crystal Structure of Apo Mada at 2.2A Resolution:
3.5.4.4;

The structure of Crystal Structure of Apo Mada at 2.2A Resolution, PDB code: 3mvt was solved by W.Niu, Q.Shu, Z.Chen, S.Mathews, E.Di Cera, C.Frieden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.90 / 2.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	98.833, 93.827, 86.180, 90.00, 96.76, 90.00
R / Rfree (%)	18.7 / 24.5

The binding sites of Chlorine atom in the Crystal Structure of Apo Mada at 2.2A Resolution (pdb code 3mvt). 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 Crystal Structure of Apo Mada at 2.2A Resolution, PDB code: 3mvt:

Chlorine binding site 1 out of 1 in the Crystal Structure of Apo Mada at 2.2A 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 Apo Mada at 2.2A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl401 b:31.5 occ:1.00 O C:HOH466 3.2 23.7 1.0 CE1 C:HIS15 3.4 22.3 1.0 CD2 C:HIS214 3.5 31.6 1.0 CB C:HIS214 3.5 27.0 1.0 NE2 C:HIS15 3.5 21.4 1.0 OD2 C:ASP181 3.8 22.4 1.0 NE2 C:HIS17 3.8 21.9 1.0 CB C:ALA183 3.8 27.5 1.0 CG C:HIS214 3.8 29.0 1.0 NH1 C:ARG101 3.8 14.6 1.0 CE1 C:HIS17 3.8 21.2 1.0 O C:HOH452 3.9 37.5 1.0 CA C:ALA183 4.2 28.5 1.0 O C:HOH362 4.4 14.2 1.0 CD C:ARG101 4.5 13.1 1.0 ND1 C:HIS15 4.5 21.8 1.0 CA C:HIS214 4.6 25.9 1.0 O C:LEU182 4.6 25.2 1.0 CG C:ASP181 4.6 21.2 1.0 OD1 C:ASP181 4.7 20.1 1.0 NE2 C:HIS238 4.7 24.5 1.0 NE2 C:HIS214 4.8 34.1 1.0 CD2 C:HIS15 4.8 20.0 1.0 CZ C:ARG101 4.9 17.3 1.0 CD2 C:HIS238 4.9 24.2 1.0 N C:HIS214 4.9 24.0 1.0

W.Niu, Q.Shu, Z.Chen, S.Mathews, E.Di Cera, C.Frieden. The Role of ZN2+ on the Structure and Stability of Murine Adenosine Deaminase. J.Phys.Chem.B V. 114 16156 2010.
ISSN: ISSN 1089-5647
PubMed: 20815357
DOI: 10.1021/JP106041V