Chlorine in PDB 6yp4: Putative Adenylyl Cyclase HPAC1 From Hippeastrum Reveals A Dominant Triphophatase Activity

The structure of Putative Adenylyl Cyclase HPAC1 From Hippeastrum Reveals A Dominant Triphophatase Activity, PDB code: 6yp4 was solved by S.Kleinboelting, C.Steegborn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.39 / 1.95
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	59.808, 59.808, 146.982, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 25.2

The structure of Putative Adenylyl Cyclase HPAC1 From Hippeastrum Reveals A Dominant Triphophatase Activity also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Chlorine atom in the Putative Adenylyl Cyclase HPAC1 From Hippeastrum Reveals A Dominant Triphophatase Activity (pdb code 6yp4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Putative Adenylyl Cyclase HPAC1 From Hippeastrum Reveals A Dominant Triphophatase Activity, PDB code: 6yp4:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Putative Adenylyl Cyclase HPAC1 From Hippeastrum Reveals A Dominant Triphophatase Activity


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Putative Adenylyl Cyclase HPAC1 From Hippeastrum Reveals A Dominant Triphophatase Activity within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:38.9 occ:1.00 O A:HOH484 2.6 35.8 1.0 O A:HOH527 3.3 49.5 1.0 CB A:HIS30 3.8 23.4 1.0 CG2 A:VAL139 3.8 30.9 1.0 CG A:ARG137 3.9 29.9 1.0 CD A:ARG137 4.0 32.7 1.0 CE2 A:TYR56 4.0 25.0 1.0 CD2 A:HIS30 4.0 27.3 1.0 CE A:LYS28 4.1 39.0 1.0 O A:ARG137 4.2 26.4 1.0 CG A:HIS30 4.2 29.6 1.0 CB A:ARG137 4.3 28.6 1.0 NE2 A:GLN32 4.3 30.5 1.0 NZ A:LYS28 4.4 36.3 1.0 N A:HIS30 4.5 21.3 1.0 CD2 A:TYR56 4.6 19.0 1.0 CA A:HIS30 4.7 24.0 1.0 CD A:LYS28 4.7 29.6 1.0 CG A:LYS28 4.8 24.3 1.0 C A:ARG137 4.9 32.2 1.0 O A:HIS30 5.0 23.9 1.0

Chlorine binding site 2 out of 3 in the Putative Adenylyl Cyclase HPAC1 From Hippeastrum Reveals A Dominant Triphophatase Activity


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Putative Adenylyl Cyclase HPAC1 From Hippeastrum Reveals A Dominant Triphophatase Activity within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl305 b:48.3 occ:1.00 O A:HOH482 2.6 47.6 1.0 O A:HOH525 2.7 42.5 1.0 NH1 A:ARG52 3.2 28.6 1.0 CZ A:PHE36 3.6 24.3 1.0 O A:HOH556 3.8 35.2 1.0 CZ A:PHE133 3.8 29.0 1.0 CD A:ARG52 3.9 37.9 1.0 CE2 A:PHE36 4.2 23.0 1.0 CB A:LYS195 4.2 29.9 1.0 N A:PHE196 4.2 31.1 1.0 CZ A:ARG52 4.3 28.3 1.0 O3G A:GCP301 4.4 72.8 1.0 CB A:PHE196 4.5 35.0 1.0 NE A:ARG52 4.6 35.2 1.0 CE2 A:PHE133 4.6 31.9 1.0 CA A:PHE196 4.6 34.2 1.0 CD A:LYS195 4.7 33.2 1.0 CE1 A:PHE133 4.7 26.4 1.0 C A:LYS195 4.7 35.8 1.0 O2G A:GCP301 4.7 55.1 1.0 CE1 A:PHE36 4.8 28.1 1.0 O1B A:GCP301 4.9 43.2 1.0 NH2 A:ARG54 4.9 32.8 1.0 CG A:ASN34 4.9 28.9 1.0 CA A:LYS195 4.9 28.4 1.0 ND2 A:ASN34 4.9 34.2 1.0 CG A:LYS195 4.9 33.5 1.0

Chlorine binding site 3 out of 3 in the Putative Adenylyl Cyclase HPAC1 From Hippeastrum Reveals A Dominant Triphophatase Activity


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Putative Adenylyl Cyclase HPAC1 From Hippeastrum Reveals A Dominant Triphophatase Activity within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl306 b:47.3 occ:1.00 OG A:SER13 3.1 27.9 1.0 N A:ALA14 3.6 32.4 1.0 O A:HOH503 3.8 37.0 1.0 CA A:ALA14 3.8 32.4 1.0 C A:SER13 3.9 34.0 1.0 CB A:SER13 4.0 32.1 1.0 CB A:ALA14 4.1 26.6 1.0 O A:SER13 4.2 30.3 1.0 CD A:PRO187 4.3 38.9 1.0 CD1 A:LEU17 4.4 26.1 1.0 CG A:PRO187 4.4 44.5 1.0 OG A:SER11 4.4 26.0 1.0 CA A:SER13 4.6 28.4 1.0

S.Kleinboelting, J.Miehling, C.Steegborn. Crystal Structure and Enzymatic Characterization of the Putative Adenylyl Cyclase HPAC1 From Hippeastrum Reveal Dominant Triphosphatase Activity. J.Struct.Biol. V. 212 07649 2020.
ISSN: ESSN 1095-8657
PubMed: 33075486
DOI: 10.1016/J.JSB.2020.107649