Chlorine in PDB 3c15: Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg

Enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg

All present enzymatic activity of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg:
4.6.1.1;

Protein crystallography data

The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg, PDB code: 3c15 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)*	24.49 / 2.78
*Space group*	P 2₁ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	117.510, 133.080, 70.108, 90.00, 90.00, 90.00
*R / R_free (%)*	23.7 / 29.1

Other elements in 3c15:

The structure of Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg (pdb code 3c15). 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-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg, PDB code: 3c15:

Chlorine binding site 1 out of 1 in 3c15

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Chlorine Binding Sites List in 3c15

Chlorine binding site 1 out of 1 in the Complex of Gs-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg

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-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Pyrophosphate and Mg within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
C:Cl403 b:49.0 occ:1.00	N	C:ALA249	3.4	31.6	1.0
	CB	C:ALA48	3.6	35.4	1.0
	CB	C:SER51	3.7	33.6	1.0
	CB	C:ALA249	3.7	33.1	1.0
	CA	C:SER51	4.0	33.9	1.0
	CA	C:ALA249	4.1	30.7	1.0
	CB	C:ALA269	4.1	39.3	1.0
	CA	C:VAL248	4.2	30.5	1.0
	N	C:ALA48	4.2	41.6	1.0
	C	C:VAL248	4.3	30.3	1.0
	O	C:ARG265	4.3	38.4	1.0
	CA	C:ALA48	4.4	39.7	1.0
	O	C:VAL247	4.4	31.4	1.0
	N	C:SER51	4.6	34.5	1.0
	C	C:ALA48	4.7	40.5	1.0
	O	C:GLY49	4.7	30.4	1.0
	O	C:ALA48	4.7	39.3	1.0
	O	C:ALA249	4.9	32.5	1.0
	C	C:ALA249	4.9	34.1	1.0
	OG	C:SER51	4.9	30.6	1.0
	CG1	C:VAL248	5.0	36.8	1.0

Reference:

T.C.Mou, N.Masada, D.M.Cooper, S.R.Sprang. Structural Basis For Inhibition of Mammalian Adenylyl Cyclase By Calcium. Biochemistry V. 48 3387 2009.
ISSN: ISSN 0006-2960
PubMed: 19243146
DOI: 10.1021/BI802122K

Page generated: Sat Dec 12 09:34:01 2020

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