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Chlorine in PDB 2gvz: Crystal Structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Atp and Mn

Enzymatic activity of Crystal Structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Atp and Mn

All present enzymatic activity of Crystal Structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Atp and Mn:
4.6.1.1;

Protein crystallography data

The structure of Crystal Structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Atp and Mn, PDB code: 2gvz was solved by T.-C.Mou, S.R.Sprang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.97 / 3.27
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 116.800, 132.100, 69.600, 90.00, 90.00, 90.00
R / Rfree (%) 27.5 / 33

Other elements in 2gvz:

The structure of Crystal Structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Atp and Mn also contains other interesting chemical elements:

Manganese (Mn) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Atp and Mn (pdb code 2gvz). 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 Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Atp and Mn, PDB code: 2gvz:

Chlorine binding site 1 out of 1 in 2gvz

Go back to Chlorine Binding Sites List in 2gvz
Chlorine binding site 1 out of 1 in the Crystal Structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Atp and Mn


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 Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Mant-Atp and Mn within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl397

b:60.0
occ:1.00
 CB C:ALA269 3.1 44.9 1.0
O C:ARG265 3.2 43.3 1.0
CB C:ALA48 3.6 56.7 1.0
CG1 C:VAL248 3.6 21.4 1.0
N C:ALA249 3.6 26.1 1.0
C C:ARG265 3.8 42.4 1.0
OG C:SER51 4.0 52.8 1.0
CB C:ALA249 4.1 31.3 1.0
CA C:LEU266 4.1 40.4 1.0
N C:LEU266 4.2 40.3 1.0
CA C:ALA269 4.3 42.9 1.0
CB C:ARG265 4.3 45.9 1.0
CA C:ALA249 4.4 28.1 1.0
CA C:VAL248 4.5 21.8 1.0
O C:ALA249 4.5 28.2 1.0
C C:VAL248 4.5 23.9 1.0
N C:ALA269 4.6 42.0 1.0
CB C:SER252 4.6 31.1 1.0
CA C:ARG265 4.6 43.2 1.0
CD1 C:LEU266 4.7 30.7 1.0
CB C:VAL248 4.7 27.3 1.0
C C:ALA249 4.8 28.3 1.0
O C:LEU266 4.8 45.1 1.0
CA C:ALA48 4.9 54.7 1.0
C C:LEU266 4.9 43.3 1.0
N C:ALA48 5.0 49.6 1.0

Reference:

T.-C.Mou, A.Gille, S.Suryanarayana, M.Richter, R.Seifert, S.R.Sprang. Broad Specificity of Mammalian Adenylyl Cyclase For Interaction with 2',3'-Substituted Purine- and Pyrimidine Nucleotide Inhibitors. Mol.Pharmacol. V. 70 878 2006.
ISSN: ISSN 0026-895X
PubMed: 16766715
DOI: 10.1124/MOL.106.026427
Page generated: Sat Jul 20 07:40:17 2024

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