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Chlorine in PDB 1xkk: Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016

Enzymatic activity of Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016

All present enzymatic activity of Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016:
2.7.1.112;

Protein crystallography data

The structure of Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016, PDB code: 1xkk was solved by E.R.Wood, A.T.Truesdale, O.B.Mcdonald, D.Yuan, A.Hassell, S.H.Dickerson, B.Ellis, C.Pennisi, E.Horne, K.Lackey, K.J.Alligood, D.W.Rusnak, T.M.Gilmer, L.M.Shewchuk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.44 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.653, 67.144, 102.880, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 25.5

Other elements in 1xkk:

The structure of Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016 also contains other interesting chemical elements:

Fluorine (F) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016 (pdb code 1xkk). 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 Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016, PDB code: 1xkk:

Chlorine binding site 1 out of 1 in 1xkk

Go back to Chlorine Binding Sites List in 1xkk
Chlorine binding site 1 out of 1 in the Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Egfr Kinase Domain Complexed with A Quinazoline Inhibitor- GW572016 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl91

b:34.7
occ:1.00
 CL3 A:FMM91 0.0 34.7 1.0
C36 A:FMM91 1.7 33.0 1.0
C26 A:FMM91 2.6 32.8 1.0
C38 A:FMM91 2.7 32.3 1.0
O27 A:FMM91 2.9 32.7 1.0
O A:LEU788 3.1 35.7 1.0
CB A:LYS745 3.4 34.4 1.0
C A:LEU788 3.6 36.3 1.0
CG2 A:THR790 3.6 31.2 1.0
N A:LYS745 3.6 33.1 1.0
O A:ALA743 3.7 30.7 1.0
CB A:LEU788 3.8 34.2 1.0
C25 A:FMM91 3.9 31.4 1.0
C23 A:FMM91 4.0 33.2 1.0
CA A:LYS745 4.1 34.3 1.0
CB A:THR790 4.2 32.7 1.0
N A:ILE789 4.2 34.8 1.0
N A:THR790 4.2 33.8 1.0
C28 A:FMM91 4.3 34.2 1.0
CA A:LEU788 4.3 36.1 1.0
C A:ALA743 4.3 31.1 1.0
CA A:ILE789 4.3 33.4 1.0
C A:ILE744 4.3 32.6 1.0
C A:ILE789 4.4 33.8 1.0
C24 A:FMM91 4.5 32.0 1.0
C35 A:FMM91 4.5 33.7 1.0
CA A:ILE744 4.5 30.6 1.0
N A:ILE744 4.7 31.7 1.0
CD A:LYS745 4.7 35.1 1.0
CG A:LYS745 4.7 34.4 1.0
CD1 A:LEU777 4.7 35.0 1.0
CA A:THR790 4.9 32.4 1.0
CB A:ALA743 4.9 31.4 1.0
C29 A:FMM91 4.9 33.4 1.0

Reference:

E.R.Wood, A.T.Truesdale, O.B.Mcdonald, D.Yuan, A.Hassell, S.H.Dickerson, B.Ellis, C.Pennisi, E.Horne, K.Lackey, K.J.Alligood, D.W.Rusnak, T.M.Gilmer, L.Shewchuk. A Unique Structure For Epidermal Growth Factor Receptor Bound to GW572016 (Lapatinib): Relationships Among Protein Conformation, Inhibitor Off-Rate, and Receptor Activity in Tumor Cells. Cancer Res. V. 64 6652 2004.
ISSN: ISSN 0008-5472
PubMed: 15374980
DOI: 10.1158/0008-5472.CAN-04-1168
Page generated: Sat Dec 12 08:54:42 2020

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