Sodium in PDB 2ahs: Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta

Enzymatic activity of Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta:
3.1.3.48;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta, PDB code: 2ahs was solved by E.Ugochukwu, J.Eswaran, A.Barr, O.Gileadi, F.Sobott, N.Burgess, L.Ball, J.Bray, F.Von Delft, J.Debreczeni, G.Bunkoczi, A.Turnbull, S.Das, J.Weigelt, A.Edwards, C.Arrowsmith, M.Sundstrom, S.Knapp, Structuralgenomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	53.40 / 2.10
*Space group*	P 6₁ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	123.368, 123.368, 179.569, 90.00, 90.00, 120.00
*R / R_free (%)*	15.2 / 20.6

Other elements in 2ahs:

The structure of Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta also contains other interesting chemical elements:

Chlorine

(Cl)

9 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta (pdb code 2ahs). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta, PDB code: 2ahs:

Sodium binding site 1 out of 1 in 2ahs

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Sodium Binding Sites List in 2ahs

Sodium binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the Catalytic Domain of Human Tyrosine Receptor Phosphatase Beta within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Na811 b:38.2 occ:1.00	O	A:ARG1743	2.8	16.5	1.0
	O	A:HOH239	3.3	36.3	1.0
	O	A:ALA1741	3.5	18.6	1.0
	O	A:HOH16	3.7	42.3	1.0
	N	A:ARG1743	3.7	15.9	1.0
	C	A:THR1742	3.8	18.9	1.0
	C	A:ARG1743	3.8	17.4	1.0
	CA	A:THR1742	3.9	18.7	1.0
	C	A:ALA1741	3.9	14.3	1.0
	N	A:THR1742	4.0	20.8	1.0
	O	A:ASP1740	4.1	17.6	1.0
	O	A:THR1742	4.3	17.2	1.0
	CA	A:ARG1743	4.3	18.3	1.0
	CE2	A:TYR1762	4.5	16.8	1.0
	CD2	A:TYR1762	4.5	20.7	1.0
	CE	A:LYS1745	4.5	43.7	1.0
	CG	A:ARG1743	4.6	14.2	1.0
	NH2	A:ARG1770	4.6	44.6	1.0
	CA	A:ALA1741	5.0	25.1	1.0
	N	A:VAL1744	5.0	15.5	1.0

Reference:

A.J.Barr, E.Ugochukwu, W.H.Lee, O.N.King, P.Filippakopoulos, I.Alfano, P.Savitsky, N.A.Burgess-Brown, S.Muller, S.Knapp. Large-Scale Structural Analysis of the Classical Human Protein Tyrosine Phosphatome. Cell(Cambridge,Mass.) V. 136 352 2009.
ISSN: ISSN 0092-8674
PubMed: 19167335
DOI: 10.1016/J.CELL.2008.11.038

Page generated: Mon Oct 7 01:52:14 2024

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