Potassium in PDB 5a1g: The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp.

Enzymatic activity of The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp.

All present enzymatic activity of The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp.:
2.5.1.6;

Protein crystallography data

The structure of The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp., PDB code: 5a1g was solved by B.Murray, S.V.Antonyuk, A.Marina, S.C.Lu, J.M.Mato, S.S.Hasnain, A.L.Rojas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	58.69 / 1.83
*Space group*	I 2 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	68.390, 94.390, 117.390, 90.00, 90.00, 90.00
*R / R_free (%)*	11.982 / 17.49

Other elements in 5a1g:

The structure of The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp. also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp. (pdb code 5a1g). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp., PDB code: 5a1g:

Potassium binding site 1 out of 1 in 5a1g

Go back to

Potassium Binding Sites List in 5a1g

Potassium binding site 1 out of 1 in the The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp.

Mono view

Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of The Structure of Human MAT2A in Complex with S-Adenosylethionine and Ppnp. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:K405 b:32.3 occ:1.00	O1B	A:PPK402	2.7	20.8	1.0
	OD1	A:ASP258	2.8	19.6	1.0
	O	A:ALA259	2.9	18.7	1.0
	O	A:HOH2014	3.1	18.4	1.0
	O	A:HOH2015	3.1	24.4	1.0
	CG	A:ASP258	3.5	20.0	1.0
	O	A:HOH2274	3.6	30.4	1.0
	OD2	A:ASP258	3.6	22.4	1.0
	MG	A:MG406	3.7	18.6	1.0
	PB	A:PPK402	3.9	25.3	1.0
	C	A:ALA259	3.9	18.8	1.0
	O2B	A:PPK402	4.0	26.9	1.0
	N	A:ALA259	4.1	17.3	1.0
	CA	A:ALA259	4.4	18.2	1.0
	N9	A:S7M404	4.4	24.0	1.0
	CB	A:ALA259	4.5	18.1	1.0
	NH2	A:ARG264	4.5	19.4	1.0
	C	A:ASP258	4.6	16.7	1.0
	O3A	A:PPK402	4.8	25.9	1.0
	CB	A:ASP258	4.8	17.9	1.0
	O2A	A:PPK402	5.0	24.8	1.0

Reference:

B.Murray, S.V.Antonyuk, A.Marina, S.C.Lu, J.M.Mato, S.S.Hasnain, A.L.Rojas. Crystallography Captures Catalytic Steps in Human Methionine Adenosyltransferase Enzymes. Proc.Natl.Acad.Sci.Usa V. 113 2104 2016.
ISSN: ISSN 0027-8424
PubMed: 26858410
DOI: 10.1073/PNAS.1510959113

Page generated: Mon Aug 12 12:50:50 2024

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