Chlorine in PDB 2yd3: Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma

Enzymatic activity of Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma

All present enzymatic activity of Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma:
3.1.3.48;

Protein crystallography data

The structure of Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma, PDB code: 2yd3 was solved by C.H.Coles, Y.Shen, A.P.Tenney, C.Siebold, G.C.Sutton, W.Lu, J.T.Gallagher, E.Y.Jones, J.G.Flanagan, A.R.Aricescu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	32.957 / 2.30
*Space group*	I 4₁ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	104.218, 104.218, 94.850, 90.00, 90.00, 90.00
*R / R_free (%)*	20.07 / 23.5

Other elements in 2yd3:

The structure of Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma also contains other interesting chemical elements:

Sodium

(Na)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma (pdb code 2yd3). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma, PDB code: 2yd3:

Chlorine binding site 1 out of 1 in 2yd3

Go back to

Chlorine Binding Sites List in 2yd3

Chlorine binding site 1 out of 1 in the Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the N-Terminal IG1-2 Module of Human Receptor Protein Tyrosine Phosphatase Sigma within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1230 b:33.2 occ:1.00	N	A:LEU155	3.3	26.9	1.0
	N	A:GLN142	3.5	29.7	1.0
	CA	A:PRO141	3.8	27.8	1.0
	CA	A:MET154	4.0	31.4	1.0
	C	A:MET154	4.1	30.6	1.0
	CB	A:LEU155	4.1	29.5	1.0
	C	A:PRO141	4.2	32.0	1.0
	CA	A:LEU155	4.2	29.6	1.0
	O	A:LEU155	4.3	34.1	1.0
	O	A:GLN142	4.4	34.3	1.0
	CB	A:PRO141	4.4	20.9	1.0
	O	A:THR153	4.4	23.3	1.0
	CA	A:GLN142	4.5	35.8	1.0
	CB	A:MET154	4.5	34.1	1.0
	CB	A:GLN142	4.5	37.6	1.0
	CG	A:MET154	4.6	38.0	1.0
	C	A:LEU155	4.7	31.0	1.0
	CD1	A:LEU155	4.7	28.7	1.0
	O	A:GLY140	4.8	32.4	1.0
	C	A:GLN142	4.9	35.9	1.0
	N	A:PRO141	4.9	26.8	1.0

Reference:

C.H.Coles, Y.Shen, A.P.Tenney, C.Siebold, G.C.Sutton, W.Lu, J.T.Gallagher, E.Y.Jones, J.G.Flanagan, A.R.Aricescu. Proteoglycan-Specific Molecular Switch For Rptp Sigma Clustering and Neuronal Extension. Science V. 332 484 2011.
ISSN: ISSN 0036-8075
PubMed: 21454754
DOI: 10.1126/SCIENCE.1200840

Page generated: Fri Jul 11 02:35:21 2025

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