Chlorine in PDB 4wp3: Crystal Structure of Adenylyl Cyclase From Mycobacterium Avium MA1120 Wild Type

All present enzymatic activity of Crystal Structure of Adenylyl Cyclase From Mycobacterium Avium MA1120 Wild Type:
4.6.1.1;

The structure of Crystal Structure of Adenylyl Cyclase From Mycobacterium Avium MA1120 Wild Type, PDB code: 4wp3 was solved by D.V.Barathy, N.G.Bharambe, K.Suguna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.21 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	97.790, 53.870, 111.200, 90.00, 94.77, 90.00
R / Rfree (%)	17.8 / 21.4

The binding sites of Chlorine atom in the Crystal Structure of Adenylyl Cyclase From Mycobacterium Avium MA1120 Wild Type (pdb code 4wp3). 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 Adenylyl Cyclase From Mycobacterium Avium MA1120 Wild Type, PDB code: 4wp3:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Adenylyl Cyclase From Mycobacterium Avium MA1120 Wild Type


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 Adenylyl Cyclase From Mycobacterium Avium MA1120 Wild Type within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl301 b:42.6 occ:1.00 H C:LYS205 2.3 27.1 1.0 HE21 C:GLN172 2.4 37.4 1.0 HA C:LEU204 2.8 27.5 1.0 NE C:ARG168 3.1 33.1 1.0 N C:LYS205 3.2 27.1 1.0 NE2 C:GLN172 3.2 37.4 1.0 HD23 C:LEU204 3.3 31.1 1.0 HG2 C:GLN172 3.4 33.6 1.0 HB3 C:ARG168 3.4 14.4 1.0 HB3 C:LYS205 3.5 34.4 1.0 HD22 C:LEU204 3.5 31.1 1.0 HE22 C:GLN172 3.6 37.4 1.0 CA C:LEU204 3.6 27.5 1.0 HB2 C:LYS205 3.7 34.4 1.0 HB3 C:LEU204 3.8 18.3 1.0 CD2 C:LEU204 3.9 31.1 1.0 C C:LEU204 3.9 23.9 1.0 CB C:LYS205 3.9 34.4 1.0 HB3 C:ALA171 4.1 23.8 1.0 O C:HOH526 4.1 51.4 1.0 CG C:GLN172 4.1 33.6 1.0 CA C:LYS205 4.2 34.6 1.0 CD C:GLN172 4.2 31.6 1.0 HA C:ARG168 4.2 12.2 1.0 CB C:LEU204 4.2 18.3 1.0 O C:ARG168 4.2 17.2 1.0 CB C:ARG168 4.2 14.4 1.0 O C:GLU203 4.3 28.2 1.0 CD C:ARG168 4.3 35.4 1.0 HG3 C:ARG168 4.4 22.9 1.0 HG3 C:GLN172 4.4 33.6 1.0 CG C:ARG168 4.6 22.9 1.0 HD21 C:LEU204 4.6 31.1 1.0 CA C:ARG168 4.6 12.2 1.0 CG C:LEU204 4.7 25.1 1.0 HA C:LYS205 4.8 34.6 1.0 N C:LEU204 4.8 24.4 1.0 HB1 C:ALA171 4.8 23.8 1.0 C C:ARG168 4.8 14.0 1.0 HD3 C:ARG168 4.9 35.4 1.0 CB C:ALA171 4.9 23.8 1.0 HD2 C:ARG168 4.9 35.4 1.0 C C:GLU203 5.0 29.0 1.0 HB2 C:ARG168 5.0 14.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Adenylyl Cyclase From Mycobacterium Avium MA1120 Wild Type


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 Adenylyl Cyclase From Mycobacterium Avium MA1120 Wild Type within 5.0Å range: probe atom residue distance (Å) B Occ F:Cl301 b:48.0 occ:1.00 HE21 F:GLN172 2.1 44.8 1.0 HH21 F:ARG168 2.3 58.0 1.0 HE F:ARG168 2.5 56.1 1.0 H F:LYS205 2.8 52.0 1.0 NE2 F:GLN172 3.0 44.8 1.0 NH2 F:ARG168 3.1 58.0 1.0 HA F:LEU204 3.1 35.6 1.0 NE F:ARG168 3.2 56.1 1.0 O F:HOH467 3.3 61.4 1.0 HB3 F:ARG168 3.3 23.7 1.0 HE22 F:GLN172 3.3 44.8 1.0 HG2 F:GLN172 3.4 31.1 1.0 HD23 F:LEU204 3.5 29.3 1.0 HD22 F:LEU204 3.5 29.3 1.0 CZ F:ARG168 3.6 62.9 1.0 N F:LYS205 3.6 52.0 1.0 HB3 F:LYS205 3.7 71.8 1.0 HH22 F:ARG168 3.8 58.0 1.0 CD2 F:LEU204 3.9 29.3 1.0 CA F:LEU204 4.0 35.6 1.0 HB3 F:LEU204 4.0 25.3 1.0 CD F:GLN172 4.0 39.7 1.0 HB3 F:ALA171 4.1 28.7 1.0 CG F:GLN172 4.1 31.1 1.0 O F:ARG168 4.1 22.1 1.0 CB F:ARG168 4.2 23.7 1.0 HA F:ARG168 4.2 22.7 1.0 C F:LEU204 4.3 47.7 1.0 HG3 F:GLN172 4.4 31.1 1.0 O F:GLU203 4.4 33.4 1.0 CB F:LEU204 4.4 25.3 1.0 HG3 F:ARG168 4.4 24.7 1.0 CD F:ARG168 4.4 41.8 1.0 CB F:LYS205 4.5 71.8 1.0 CA F:LYS205 4.6 52.1 1.0 CA F:ARG168 4.6 22.7 1.0 CG F:ARG168 4.6 24.7 1.0 O F:LYS205 4.6 57.0 1.0 HD21 F:LEU204 4.7 29.3 1.0 HB2 F:LYS205 4.7 71.8 1.0 C F:ARG168 4.7 19.8 1.0 CG F:LEU204 4.8 23.5 1.0 HB1 F:ALA171 4.8 28.7 1.0 HB2 F:ARG168 4.9 23.7 1.0 CB F:ALA171 4.9 28.7 1.0 NH1 F:ARG168 4.9 59.2 1.0 HD3 F:ARG168 5.0 41.8 1.0

D.V.Barathy, N.G.Bharambe, W.Syed, A.Zaveri, S.S.Visweswariah, M.Cola Sigmaf O, S.Misquith, K.Suguna. Autoinhibitory Mechanism and Activity-Related Structural Changes in A Mycobacterial Adenylyl Cyclase J.Struct.Biol. V. 190 304 2015.
ISSN: ESSN 1095-8657
PubMed: 25916753
DOI: 10.1016/J.JSB.2015.04.013