Manganese 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 / R_free (%)*	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:

Chlorine

(Cl)

1 atom

Manganese Binding Sites:

The binding sites of Manganese 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 Manganese atom.
In total 3 binding sites of Manganese where 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:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 2gvz

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Manganese Binding Sites List in 2gvz

Manganese binding site 1 out of 3 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 Manganese with other atoms in the Mn 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
A:Mn581 b:65.0 occ:1.00	O2A	A:ONA100	2.2	83.5	1.0
	O3B	A:ONA100	2.8	64.0	1.0
	OD1	A:ASP440	3.1	77.4	1.0
	PA	A:ONA100	3.6	83.0	1.0
	C30	A:FKP1	3.8	84.1	1.0
	N2	A:FKP1	3.9	86.0	1.0
	OD1	A:ASP396	4.0	79.1	1.0
	O1A	A:ONA100	4.1	77.2	1.0
	CG	A:ASP440	4.1	76.2	1.0
	PB	A:ONA100	4.2	74.1	1.0
	C5'	A:ONA100	4.2	98.1	1.0
	C28	A:FKP1	4.3	84.0	1.0
	C2	A:ONA100	4.3	96.4	1.0
	O	A:LEU438	4.3	80.2	1.0
	N3	A:ONA100	4.3	94.2	1.0
	CB	A:CYS441	4.4	78.8	1.0
	OD2	A:ASP440	4.4	72.1	1.0
	O5'	A:ONA100	4.6	87.6	1.0
	OD2	A:ASP396	4.6	83.9	1.0
	O2B	A:ONA100	4.7	65.1	1.0
	O3A	A:ONA100	4.7	82.6	1.0
	CG	A:ASP396	4.7	81.9	1.0
	N	A:CYS441	4.8	77.7	1.0
	N	A:ASP440	5.0	78.9	1.0

Manganese binding site 2 out of 3 in 2gvz

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Manganese Binding Sites List in 2gvz

Manganese binding site 2 out of 3 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 Manganese with other atoms in the Mn binding site number 2 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
A:Mn582 b:31.4 occ:1.00	OD2	A:ASP440	2.1	72.1	1.0
	O	A:ILE397	2.3	94.3	1.0
	OD2	A:ASP396	2.4	83.9	1.0
	O1B	A:ONA100	2.5	75.7	1.0
	C	A:ILE397	2.9	93.9	1.0
	O1G	A:ONA100	3.0	61.5	1.0
	CG	A:ASP396	3.1	81.9	1.0
	N	A:ILE397	3.1	88.7	1.0
	CG	A:ASP440	3.2	76.2	1.0
	O3B	A:ONA100	3.2	64.0	1.0
	PG	A:ONA100	3.3	53.6	1.0
	PB	A:ONA100	3.3	74.1	1.0
	CA	A:ILE397	3.5	92.8	1.0
	C	A:ASP396	3.7	84.2	1.0
	OD1	A:ASP396	3.7	79.1	1.0
	O2G	A:ONA100	3.7	56.2	1.0
	CB	A:ASP396	3.8	81.8	1.0
	CB	A:ILE397	3.8	94.4	1.0
	N	A:GLU398	3.9	95.6	1.0
	OD1	A:ASP440	3.9	77.4	1.0
	CB	A:ASP440	4.0	76.3	1.0
	CB	A:PHE400	4.1	99.7	1.0
	CA	A:ASP396	4.1	80.9	1.0
	O2B	A:ONA100	4.2	65.1	1.0
	CA	A:GLU398	4.3	0.0	1.0
	O	A:ASP396	4.3	84.1	1.0
	O1A	A:ONA100	4.3	77.2	1.0
	N	A:PHE400	4.5	98.9	1.0
	CG1	A:ILE397	4.5	95.6	1.0
	N	A:GLY399	4.6	94.6	1.0
	NH2	A:ARG484	4.6	94.5	1.0
	C	A:GLU398	4.7	92.2	1.0
	O3G	A:ONA100	4.8	65.7	1.0
	CA	A:PHE400	5.0	0.4	1.0

Manganese binding site 3 out of 3 in 2gvz

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Manganese Binding Sites List in 2gvz

Manganese binding site 3 out of 3 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 Manganese with other atoms in the Mn binding site number 3 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:Mn396 b:17.8 occ:1.00	O2G	C:GSP395	2.2	74.7	1.0
	O2B	C:GSP395	2.3	54.5	1.0
	OG	C:SER54	2.3	38.2	1.0
	OG1	C:THR204	2.4	57.6	1.0
	O3G	C:GSP395	2.5	72.3	1.0
	PG	C:GSP395	2.7	73.7	1.0
	CB	C:SER54	3.2	40.0	1.0
	CB	C:THR204	3.2	58.6	1.0
	PB	C:GSP395	3.3	51.5	1.0
	OD2	C:ASP223	3.3	57.5	1.0
	O3B	C:GSP395	3.5	64.0	1.0
	O2A	C:GSP395	3.7	37.8	1.0
	N	C:THR204	3.9	61.2	1.0
	N	C:SER54	4.0	36.8	1.0
	OD1	C:ASP223	4.1	59.2	1.0
	O	C:VAL202	4.1	58.2	1.0
	CG	C:ASP223	4.1	55.6	1.0
	PA	C:GSP395	4.1	38.9	1.0
	O3A	C:GSP395	4.2	45.5	1.0
	CA	C:SER54	4.2	36.9	1.0
	CA	C:THR204	4.2	61.3	1.0
	O1A	C:GSP395	4.2	41.6	1.0
	CG2	C:THR204	4.3	55.9	1.0
	O1B	C:GSP395	4.4	56.7	1.0
	S1G	C:GSP395	4.4	76.1	1.0
	C	C:LEU203	4.8	60.2	1.0
	CB	C:LYS53	4.9	27.9	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 14:16:55 2024

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