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Chlorine in PDB 6tdq: Crystal Structure of the Disulfide Engineered Hla-A0201 Molecule in Complex with One Gm Dipeptide in the A Pocket and One Gm Dipeptide in the F Pocket.

Protein crystallography data

The structure of Crystal Structure of the Disulfide Engineered Hla-A0201 Molecule in Complex with One Gm Dipeptide in the A Pocket and One Gm Dipeptide in the F Pocket., PDB code: 6tdq was solved by R.Anjanappa, M.Garcia Alai, S.Springer, R.Meijers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 83.72 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.643, 84.124, 83.716, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 21.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Disulfide Engineered Hla-A0201 Molecule in Complex with One Gm Dipeptide in the A Pocket and One Gm Dipeptide in the F Pocket. (pdb code 6tdq). 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 the Disulfide Engineered Hla-A0201 Molecule in Complex with One Gm Dipeptide in the A Pocket and One Gm Dipeptide in the F Pocket., PDB code: 6tdq:

Chlorine binding site 1 out of 1 in 6tdq

Go back to Chlorine Binding Sites List in 6tdq
Chlorine binding site 1 out of 1 in the Crystal Structure of the Disulfide Engineered Hla-A0201 Molecule in Complex with One Gm Dipeptide in the A Pocket and One Gm Dipeptide in the F Pocket.


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 the Disulfide Engineered Hla-A0201 Molecule in Complex with One Gm Dipeptide in the A Pocket and One Gm Dipeptide in the F Pocket. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl307

b:31.7
occ:1.00
OE1 A:GLN96 2.6 16.8 1.0
N A:GLY120 2.9 16.5 1.0
O A:THR94 3.0 16.8 1.0
N A:ASP119 3.1 14.4 1.0
O A:ALA117 3.5 18.4 1.0
C A:ALA117 3.5 14.7 1.0
C A:TYR118 3.5 15.7 1.0
CD A:GLN96 3.6 15.8 1.0
CA A:TYR118 3.7 13.8 1.0
N A:TYR118 3.7 15.4 1.0
CA A:GLY120 3.7 17.7 1.0
C A:THR94 3.7 17.9 1.0
CB A:ALA117 3.7 17.4 1.0
CA A:ASP119 3.8 15.8 1.0
CG2 A:THR94 3.8 19.2 1.0
C A:ASP119 3.8 14.5 1.0
CG A:GLN96 3.8 16.7 1.0
CB A:THR94 3.8 18.1 1.0
N A:GLN96 3.9 16.0 1.0
NE2 B:HIS32 3.9 22.4 1.0
CE1 B:HIS32 4.1 18.2 1.0
CB A:GLN96 4.1 16.1 1.0
C A:VAL95 4.2 17.1 1.0
O A:TYR118 4.3 15.9 1.0
CA A:ALA117 4.3 16.7 1.0
CA A:VAL95 4.3 19.2 1.0
N A:VAL95 4.3 16.9 1.0
CA A:THR94 4.4 17.1 1.0
C A:GLY120 4.7 20.9 1.0
CA A:GLN96 4.7 16.0 1.0
N A:LYS121 4.8 19.7 1.0
NE2 A:GLN96 4.8 16.7 1.0
O A:ASP119 4.9 16.2 1.0
OG1 A:THR94 5.0 19.5 1.0

Reference:

R.Anjanappa, M.Garcia-Alai, J.D.Kopicki, J.Lockhauserbaumer, M.Aboelmagd, J.Hinrichs, I.M.Nemtanu, C.Uetrecht, M.Zacharias, S.Springer, R.Meijers. Structures of Peptide-Free and Partially Loaded Mhc Class I Molecules Reveal Mechanisms of Peptide Selection. Nat Commun V. 11 1314 2020.
ISSN: ESSN 2041-1723
PubMed: 32161266
DOI: 10.1038/S41467-020-14862-4
Page generated: Mon Jul 29 15:23:38 2024

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