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Chlorine in PDB 2zv9: Lyn Tyrosine Kinase Domain-PP2 Complex

Enzymatic activity of Lyn Tyrosine Kinase Domain-PP2 Complex

All present enzymatic activity of Lyn Tyrosine Kinase Domain-PP2 Complex:
2.7.10.2;

Protein crystallography data

The structure of Lyn Tyrosine Kinase Domain-PP2 Complex, PDB code: 2zv9 was solved by N.K.Williams, J.Rossjohn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.22 / 2.76
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 128.468, 128.468, 54.169, 90.00, 90.00, 120.00
R / Rfree (%) 19.5 / 23.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Lyn Tyrosine Kinase Domain-PP2 Complex (pdb code 2zv9). 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 Lyn Tyrosine Kinase Domain-PP2 Complex, PDB code: 2zv9:

Chlorine binding site 1 out of 1 in 2zv9

Go back to Chlorine Binding Sites List in 2zv9
Chlorine binding site 1 out of 1 in the Lyn Tyrosine Kinase Domain-PP2 Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Lyn Tyrosine Kinase Domain-PP2 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl513

b:58.4
occ:1.00
CL A:PP2513 0.0 58.4 1.0
C14 A:PP2513 1.8 56.2 1.0
C13 A:PP2513 2.8 55.8 1.0
C15 A:PP2513 2.8 56.0 1.0
CE A:MET294 3.2 13.1 1.0
OE2 A:GLU290 3.2 17.7 1.0
CG2 A:THR319 3.5 4.5 1.0
CG2 A:ILE317 3.7 4.8 1.0
CD A:GLU290 3.7 15.1 1.0
SD A:MET294 3.9 9.0 1.0
CD A:LYS275 4.0 11.4 1.0
C12 A:PP2513 4.1 54.8 1.0
C16 A:PP2513 4.1 55.1 1.0
CG A:GLU290 4.3 13.6 1.0
OE1 A:GLU290 4.3 14.8 1.0
CB A:ILE317 4.4 5.0 1.0
NZ A:LYS275 4.6 17.1 1.0
C11 A:PP2513 4.6 55.3 1.0
CB A:LYS275 4.6 9.7 1.0
CD1 A:ILE317 4.7 3.0 1.0
CB A:THR319 4.8 6.8 1.0
CE A:LYS275 4.9 14.1 1.0
CG A:LYS275 5.0 10.4 1.0

Reference:

N.K.Williams, I.S.Lucet, S.P.Klinken, E.Ingley, J.Rossjohn. Crystal Structures of the Lyn Protein Tyrosine Kinase Domain in Its Apo- and Inhibitor-Bound State J.Biol.Chem. V. 284 284 2009.
ISSN: ISSN 0021-9258
PubMed: 18984583
DOI: 10.1074/JBC.M807850200
Page generated: Fri Jul 11 02:57:07 2025

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