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Chlorine in PDB 3f3s: The Crystal Structure of Human Lambda-Crystallin, CRYL1

Protein crystallography data

The structure of The Crystal Structure of Human Lambda-Crystallin, CRYL1, PDB code: 3f3s was solved by E.Ugochukwu, C.Johansson, W.W.Yue, G.Kochan, E.Pilka, A.Kramm, A.C.W.Pike, P.Filippakopoulos, F.Von Delft, C.Bountra, C.H.Arrowsmith, J.Weigelt, A.Edwards, U.Oppermann, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.73 / 2.00
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 102.085, 102.085, 134.986, 90.00, 90.00, 120.00
R / Rfree (%) 15.4 / 19.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Crystal Structure of Human Lambda-Crystallin, CRYL1 (pdb code 3f3s). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the The Crystal Structure of Human Lambda-Crystallin, CRYL1, PDB code: 3f3s:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 3f3s

Go back to Chlorine Binding Sites List in 3f3s
Chlorine binding site 1 out of 4 in the The Crystal Structure of Human Lambda-Crystallin, CRYL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Crystal Structure of Human Lambda-Crystallin, CRYL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl318

b:70.6
occ:1.00
O A:HOH343 3.2 32.5 1.0
N A:ARG274 3.4 28.8 1.0
CB A:ARG274 3.8 32.6 1.0
CA A:SER273 3.9 28.0 1.0
CB A:SER273 4.1 35.2 1.0
C A:SER273 4.2 39.6 1.0
CA A:ARG274 4.2 29.6 1.0

Chlorine binding site 2 out of 4 in 3f3s

Go back to Chlorine Binding Sites List in 3f3s
Chlorine binding site 2 out of 4 in the The Crystal Structure of Human Lambda-Crystallin, CRYL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Crystal Structure of Human Lambda-Crystallin, CRYL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1

b:75.2
occ:1.00
N B:GLY64 3.5 31.3 1.0
CA B:GLY64 4.2 35.9 1.0
CG B:LYS63 4.3 38.3 1.0
CA B:LYS63 4.4 28.1 1.0
C B:LYS63 4.5 34.2 1.0
CB B:LYS63 5.0 35.2 1.0

Chlorine binding site 3 out of 4 in 3f3s

Go back to Chlorine Binding Sites List in 3f3s
Chlorine binding site 3 out of 4 in the The Crystal Structure of Human Lambda-Crystallin, CRYL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of The Crystal Structure of Human Lambda-Crystallin, CRYL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl318

b:90.5
occ:1.00
CE B:LYS177 3.4 60.4 1.0
CE1 B:HIS173 3.6 37.8 1.0
O B:HOH513 3.8 47.8 1.0
NE2 B:HIS173 3.8 42.2 1.0
CD B:LYS177 4.3 58.7 1.0
CG B:LYS177 4.5 60.1 1.0
ND1 B:HIS173 4.9 41.3 1.0

Chlorine binding site 4 out of 4 in 3f3s

Go back to Chlorine Binding Sites List in 3f3s
Chlorine binding site 4 out of 4 in the The Crystal Structure of Human Lambda-Crystallin, CRYL1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of The Crystal Structure of Human Lambda-Crystallin, CRYL1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl3

b:42.2
occ:1.00
O B:HOH612 3.0 42.6 1.0
O B:HOH440 3.2 31.0 1.0
N B:MET127 3.2 31.3 1.0
CE B:LYS130 3.4 35.0 1.0
CD B:LYS130 3.5 27.7 1.0
CA B:LEU126 3.8 30.4 1.0
CB B:MET127 3.9 31.3 1.0
NZ B:LYS130 3.9 39.0 1.0
CG B:MET127 4.0 34.9 1.0
C B:LEU126 4.0 30.7 1.0
CD2 B:LEU126 4.2 27.4 1.0
CA B:MET127 4.2 33.7 1.0
CG B:LYS130 4.2 39.9 1.0
NE2 A:HIS261 4.2 32.0 1.0
O B:CYS125 4.3 30.3 1.0
SD B:MET127 4.4 45.9 1.0
CB B:LEU126 4.5 24.2 1.0
CD2 A:HIS261 4.7 36.2 1.0
CB B:LYS130 4.8 34.1 1.0
CB B:ALA191 4.9 29.4 1.0
N B:LEU126 4.9 33.4 1.0
CG B:LEU126 4.9 28.9 1.0
C B:CYS125 4.9 32.5 1.0

Reference:

E.Ugochukwu, C.Johansson, W.W.Yue, G.Kochan, E.Pilka, A.Kramm, A.C.W.Pike, P.Filippakopoulos, F.Von Delft, U.Oppermann. The Crystal Structure of Human Lambda-Crystallin, CRYL1 To Be Published.
Page generated: Fri Jul 11 04:56:38 2025

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