Chlorine in PDB 2gvd: Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn

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

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

Protein crystallography data

The structure of Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn, PDB code: 2gvd 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)*	14.96 / 2.90
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	118.200, 133.400, 70.600, 90.00, 90.00, 90.00
*R / R_free (%)*	24.5 / 27.9

Other elements in 2gvd:

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

Manganese

(Mn)

3 atoms

Chlorine Binding Sites:

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

Chlorine binding site 1 out of 1 in 2gvd

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Chlorine Binding Sites List in 2gvd

Chlorine binding site 1 out of 1 in the Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-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 Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
C:Cl397 b:25.9 occ:1.00	O	C:HOH419	3.2	13.7	1.0
	N	C:ALA249	3.3	22.8	1.0
	CB	C:ALA249	3.5	27.8	1.0
	CB	C:ALA48	3.6	26.2	1.0
	O	C:ARG265	3.7	25.4	1.0
	CA	C:ALA249	4.0	24.6	1.0
	CB	C:ALA269	4.1	20.8	1.0
	CB	C:SER51	4.1	26.5	1.0
	C	C:VAL248	4.3	21.0	1.0
	CA	C:SER51	4.4	24.2	1.0
	CA	C:VAL248	4.4	19.2	1.0
	CG1	C:VAL248	4.5	13.3	1.0
	O	C:GLY49	4.6	25.7	1.0
	CA	C:ALA48	4.6	26.4	1.0
	N	C:ALA48	4.7	22.5	1.0
	C	C:ARG265	4.7	25.1	1.0
	C	C:ALA249	4.7	25.2	1.0
	O	C:ALA249	4.7	26.0	1.0
	C	C:ALA48	4.8	27.6	1.0
	CA	C:ALA269	5.0	19.6	1.0
	N	C:SER51	5.0	25.7	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 07:39:58 2024

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