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Chlorine in PDB 8sc7: Structure of Egfr in Complex with Mtx-531

Enzymatic activity of Structure of Egfr in Complex with Mtx-531

All present enzymatic activity of Structure of Egfr in Complex with Mtx-531:
2.7.10.1;

Protein crystallography data

The structure of Structure of Egfr in Complex with Mtx-531, PDB code: 8sc7 was solved by C.E.Whitehead, J.Leopold, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.30 / 1.98
Space group I 2 3
Cell size a, b, c (Å), α, β, γ (°) 145.517, 145.517, 145.517, 90, 90, 90
R / Rfree (%) 18.6 / 21.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Egfr in Complex with Mtx-531 (pdb code 8sc7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Egfr in Complex with Mtx-531, PDB code: 8sc7:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 8sc7

Go back to Chlorine Binding Sites List in 8sc7
Chlorine binding site 1 out of 2 in the Structure of Egfr in Complex with Mtx-531


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Egfr in Complex with Mtx-531 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1102

b:83.4
occ:1.00
O A:HOH1387 3.0 51.0 1.0
NH1 A:ARG803 3.1 52.9 1.0
NH2 A:ARG803 3.4 56.2 1.0
O A:HOH1390 3.5 65.6 1.0
CZ A:ARG803 3.7 54.2 1.0
CE A:LYS913 3.8 65.3 1.0
CG A:LYS913 4.3 58.3 1.0
O A:HOH1343 4.3 44.9 1.0
CD A:LYS913 4.3 62.4 1.0
CD2 A:LEU799 4.4 48.6 1.0
NZ A:LYS913 4.7 69.9 1.0
O A:HOH1274 4.8 43.6 1.0
O A:HOH1413 4.8 60.5 1.0

Chlorine binding site 2 out of 2 in 8sc7

Go back to Chlorine Binding Sites List in 8sc7
Chlorine binding site 2 out of 2 in the Structure of Egfr in Complex with Mtx-531


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Egfr in Complex with Mtx-531 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1103

b:89.3
occ:1.00
CL A:D0D1103 0.0 89.3 1.0
C8 A:D0D1103 1.7 78.6 1.0
N A:D0D1103 2.6 72.1 1.0
C9 A:D0D1103 2.7 77.8 1.0
N1 A:D0D1103 3.1 80.2 0.3
N1 A:D0D1103 3.2 80.8 0.3
N1 A:D0D1103 3.2 81.9 0.3
O A:LEU718 3.4 85.0 1.0
O A:HOH1203 3.8 76.8 1.0
C7 A:D0D1103 3.8 67.1 1.0
C10 A:D0D1103 4.0 71.4 1.0
CA A:GLY719 4.2 82.5 1.0
C A:LEU718 4.3 80.5 1.0
O1 A:GOL1101 4.4 89.8 1.0
C6 A:D0D1103 4.4 63.4 1.0
O A:HOH1223 4.4 83.0 1.0
O A:HOH1331 4.5 73.8 1.0
O A:HOH1378 4.5 77.4 1.0
S A:D0D1103 4.5 83.9 0.3
S A:D0D1103 4.5 82.6 0.3
N A:GLY719 4.6 81.2 1.0
S A:D0D1103 4.6 81.3 0.3
C11 A:D0D1103 4.7 81.5 0.3
O A:D0D1103 4.8 78.7 0.3
O A:D0D1103 4.8 86.3 0.3
O1 A:D0D1103 4.8 77.6 0.3
O1 A:D0D1103 4.9 84.5 0.3

Reference:

C.E.Whitehead, J.Leopold. Structure of Egfr in Complex with Mtx-531 To Be Published.
Page generated: Sun Jul 13 14:05:46 2025

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