Manganese in PDB 1phk: Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product

Enzymatic activity of Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product

All present enzymatic activity of Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product:
2.7.1.38;

Protein crystallography data

The structure of Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product, PDB code: 1phk was solved by D.J.Owen, M.E.M.Noble, E.F.Garman, A.C.Papageorgiou, L.N.Johnson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	6.00 / 2.20
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	47.600, 67.400, 110.800, 90.00, 90.00, 90.00
*R / R_free (%)*	21 / 28.8

Manganese Binding Sites:

The binding sites of Manganese atom in the Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product (pdb code 1phk). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product, PDB code: 1phk:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1phk

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Manganese Binding Sites List in 1phk

Manganese binding site 1 out of 2 in the Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product

Mono view

Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mn382 b:44.7 occ:1.00	O	A:HOH446	2.2	49.9	1.0
	OD1	A:ASP167	2.4	37.3	1.0
	O2B	A:ATP381	2.4	43.6	1.0
	O3G	A:ATP381	2.5	51.2	1.0
	OD2	A:ASP167	2.5	35.3	1.0
	CG	A:ASP167	2.8	34.3	1.0
	O3B	A:ATP381	3.3	48.5	1.0
	PG	A:ATP381	3.4	59.1	1.0
	PB	A:ATP381	3.4	41.4	1.0
	MN	A:MN383	3.9	32.4	1.0
	O2G	A:ATP381	3.9	45.7	1.0
	O	A:HOH469	4.1	84.1	1.0
	OD2	A:ASP149	4.2	38.7	1.0
	CB	A:ASP167	4.2	28.2	1.0
	O1B	A:ATP381	4.4	43.9	1.0
	NZ	A:LYS48	4.4	33.8	1.0
	CA	A:GLY169	4.4	24.5	1.0
	O2A	A:ATP381	4.5	42.3	1.0
	O3A	A:ATP381	4.5	31.9	1.0
	N	A:GLY169	4.6	23.1	1.0
	O1G	A:ATP381	4.6	54.6	1.0
	PA	A:ATP381	4.9	34.7	1.0
	CE1	A:PHE170	5.0	32.0	1.0
	CA	A:ASP167	5.0	29.5	1.0

Manganese binding site 2 out of 2 in 1phk

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Manganese Binding Sites List in 1phk

Manganese binding site 2 out of 2 in the Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product

Mono view

Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Two Structures of the Catalytic Domain of Phosphorylase, Kinase: An Active Protein Kinase Complexed with Nucleotide, Substrate-Analogue and Product within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mn383 b:32.4 occ:1.00	OD1	A:ASN154	2.3	26.6	1.0
	O2G	A:ATP381	2.3	45.7	1.0
	O2A	A:ATP381	2.4	42.3	1.0
	OD2	A:ASP167	2.4	35.3	1.0
	O	A:HOH403	2.5	37.7	1.0
	O3B	A:ATP381	2.6	48.5	1.0
	PG	A:ATP381	2.9	59.1	1.0
	CG	A:ASN154	3.3	27.1	1.0
	CG	A:ASP167	3.3	34.3	1.0
	NZ	A:LYS151	3.5	59.9	1.0
	PA	A:ATP381	3.6	34.7	1.0
	O3G	A:ATP381	3.7	51.2	1.0
	ND2	A:ASN154	3.7	30.9	1.0
	PB	A:ATP381	3.8	41.4	1.0
	CB	A:ASP167	3.9	28.2	1.0
	MN	A:MN382	3.9	44.7	1.0
	O3A	A:ATP381	3.9	31.9	1.0
	O2B	A:ATP381	4.1	43.6	1.0
	O1G	A:ATP381	4.2	54.6	1.0
	O	A:HOH532	4.2	76.3	1.0
	OD1	A:ASP167	4.3	37.3	1.0
	O5'	A:ATP381	4.6	46.0	1.0
	C5'	A:ATP381	4.6	36.1	1.0
	O1A	A:ATP381	4.6	34.4	1.0
	CB	A:ASN154	4.7	24.8	1.0
	OD2	A:ASP149	4.7	38.7	1.0
	CE	A:LYS151	4.7	58.1	1.0
	O3'	A:ATP381	4.7	35.7	1.0
	O	A:GLU153	4.8	37.6	1.0
	CA	A:ASN154	5.0	29.3	1.0

Reference:

D.J.Owen, M.E.Noble, E.F.Garman, A.C.Papageorgiou, L.N.Johnson. Two Structures of the Catalytic Domain of Phosphorylase Kinase: An Active Protein Kinase Complexed with Substrate Analogue and Product. Structure V. 3 467 1995.
ISSN: ISSN 0969-2126
PubMed: 7663944
DOI: 10.1016/S0969-2126(01)00180-0

Page generated: Sat Oct 5 12:05:16 2024

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