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Chlorine in PDB 3ad4: Crystal Structure of Methoxy Benzofuran Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394)

Enzymatic activity of Crystal Structure of Methoxy Benzofuran Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394)

All present enzymatic activity of Crystal Structure of Methoxy Benzofuran Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394):
2.7.10.2;

Protein crystallography data

The structure of Crystal Structure of Methoxy Benzofuran Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394), PDB code: 3ad4 was solved by E.Tsuji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.277, 73.612, 92.760, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 25.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Methoxy Benzofuran Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394) (pdb code 3ad4). 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 Methoxy Benzofuran Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394), PDB code: 3ad4:

Chlorine binding site 1 out of 1 in 3ad4

Go back to Chlorine Binding Sites List in 3ad4
Chlorine binding site 1 out of 1 in the Crystal Structure of Methoxy Benzofuran Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394)


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 Methoxy Benzofuran Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1

b:70.8
occ:1.00
CL1 A:KBM1 0.0 70.8 1.0
C2 A:KBM1 1.8 71.5 1.0
C3 A:KBM1 2.8 71.3 1.0
C5 A:KBM1 2.9 70.7 1.0
O A:HOH85 3.5 20.5 1.0
C4 A:KBM1 4.1 70.3 1.0
C6 A:KBM1 4.2 69.3 1.0
O A:HOH173 4.2 36.6 1.0
OE2 A:GLU288 4.4 35.0 1.0
CD A:LYS273 4.5 26.4 1.0
OG1 A:THR316 4.6 17.6 1.0
CE A:LYS273 4.6 29.5 1.0
NZ A:LYS273 4.6 31.1 1.0
C7 A:KBM1 4.7 69.2 1.0
O A:HOH140 4.7 36.9 1.0
CG2 A:THR316 4.7 14.2 1.0
O A:HOH2 4.9 26.2 1.0

Reference:

M.Ozawa, T.Ozawa, E.Tsuji, K.Okazaki, K.Takeda. Ab Initio Fragment Molecular Orbital Study of Ligand Binding to Leukocyte-Specific Protein Tyrosine (Lck) Kinase To Be Published.
Page generated: Sat Dec 12 09:31:14 2020

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