Manganese 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:

Chlorine

(Cl)

1 atom

Manganese Binding Sites:

The binding sites of Manganese 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 Manganese atom.
In total 3 binding sites of Manganese where determined in the Complex of Gs- with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Tnp-Atp and Mn, PDB code: 2gvd:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 2gvd

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Manganese Binding Sites List in 2gvd

Manganese binding site 1 out of 3 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 Manganese with other atoms in the Mn 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
A:Mn581 b:56.8 occ:1.00	OD1	A:ASP440	2.4	49.7	1.0
	OD1	A:ASP396	3.3	44.5	1.0
	OD2	A:ASP396	3.3	38.0	1.0
	CG	A:ASP440	3.4	47.2	1.0
	CG	A:ASP396	3.6	38.5	1.0
	O1A	A:128584	3.7	64.5	1.0
	MN	A:MN582	3.8	20.4	1.0
	OD2	A:ASP440	3.8	46.8	1.0
	C5'	A:128584	3.9	70.0	1.0
	CB	A:CYS441	4.2	48.2	1.0
	N	A:CYS441	4.4	45.4	1.0
	O	A:LEU438	4.5	37.9	1.0
	C30	A:FKP583	4.5	64.1	1.0
	C	A:ASP440	4.6	45.6	1.0
	O4'	A:128584	4.6	70.5	1.0
	N	A:ASP440	4.6	45.0	1.0
	CB	A:ASP440	4.7	46.3	1.0
	O5'	A:128584	4.8	72.2	1.0
	CA	A:CYS441	4.8	46.2	1.0
	PA	A:128584	4.9	71.9	1.0
	C4'	A:128584	4.9	69.4	1.0
	CA	A:ASP440	4.9	46.4	1.0
	CB	A:ASP396	4.9	39.7	1.0
	O2B	A:128584	5.0	69.3	1.0
	O	A:ASP440	5.0	44.5	1.0

Manganese binding site 2 out of 3 in 2gvd

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Manganese Binding Sites List in 2gvd

Manganese binding site 2 out of 3 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 Manganese with other atoms in the Mn binding site number 2 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
A:Mn582 b:20.4 occ:1.00	OD2	A:ASP440	2.2	46.8	1.0
	O2B	A:128584	2.3	69.3	1.0
	OD2	A:ASP396	2.4	38.0	1.0
	O	A:ILE397	2.4	44.7	1.0
	O3B	A:128584	2.6	66.0	1.0
	OD1	A:ASP396	2.6	44.5	1.0
	CG	A:ASP396	2.7	38.5	1.0
	PB	A:128584	2.7	66.8	1.0
	CG	A:ASP440	3.2	47.2	1.0
	C	A:ILE397	3.4	47.5	1.0
	OD1	A:ASP440	3.5	49.7	1.0
	N	A:ILE397	3.7	47.2	1.0
	O1B	A:128584	3.8	60.2	1.0
	MN	A:MN581	3.8	56.8	1.0
	O3A	A:128584	3.9	68.5	1.0
	PG	A:128584	4.0	65.9	1.0
	CA	A:ILE397	4.0	47.2	1.0
	CB	A:ASP396	4.0	39.7	1.0
	C	A:ASP396	4.2	44.5	1.0
	O1A	A:128584	4.3	64.5	1.0
	CB	A:ILE397	4.3	47.2	1.0
	O2G	A:128584	4.4	66.4	1.0
	C5'	A:128584	4.4	70.0	1.0
	CB	A:ASP440	4.5	46.3	1.0
	N	A:GLU398	4.5	50.0	1.0
	CA	A:ASP396	4.6	40.3	1.0
	PA	A:128584	4.7	71.9	1.0
	CB	A:PHE400	4.7	56.5	1.0
	NH1	A:ARG484	4.8	46.4	1.0
	N	A:GLY399	4.8	55.3	1.0
	O1G	A:128584	4.8	70.2	1.0
	CA	A:GLU398	4.8	54.0	1.0
	O	A:ASP440	4.9	44.5	1.0
	N	A:PHE400	4.9	57.5	1.0
	O	A:ASP396	4.9	45.2	1.0

Manganese binding site 3 out of 3 in 2gvd

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Manganese Binding Sites List in 2gvd

Manganese binding site 3 out of 3 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 Manganese with other atoms in the Mn binding site number 3 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:Mn396 b:40.2 occ:1.00	O2B	C:GSP395	2.1	38.3	1.0
	O2G	C:GSP395	2.3	60.9	1.0
	OG1	C:THR204	2.3	30.9	1.0
	OG	C:SER54	2.3	26.1	1.0
	CB	C:THR204	3.0	29.7	1.0
	PG	C:GSP395	3.1	59.7	1.0
	PB	C:GSP395	3.2	34.4	1.0
	CB	C:SER54	3.3	24.8	1.0
	O3G	C:GSP395	3.4	61.6	1.0
	O3B	C:GSP395	3.5	49.1	1.0
	OD1	C:ASP223	3.7	53.6	1.0
	N	C:SER54	3.8	22.1	1.0
	CG2	C:THR204	3.9	27.8	1.0
	CA	C:SER54	4.1	24.2	1.0
	O2A	C:GSP395	4.1	28.1	1.0
	O1B	C:GSP395	4.1	37.4	1.0
	N	C:THR204	4.2	34.0	1.0
	OD2	C:ASP223	4.2	53.9	1.0
	CA	C:THR204	4.2	32.6	1.0
	O3A	C:GSP395	4.3	34.6	1.0
	CG	C:ASP223	4.4	49.2	1.0
	PA	C:GSP395	4.5	30.4	1.0
	O	C:VAL202	4.5	33.3	1.0
	CE	C:LYS53	4.6	23.1	1.0
	CB	C:LYS53	4.6	22.3	1.0
	O1A	C:GSP395	4.6	34.6	1.0
	O	C:VAL224	4.9	29.4	1.0
	S1G	C:GSP395	4.9	56.7	1.0
	C	C:LYS53	4.9	21.4	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 Oct 5 14:16:48 2024

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