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Sodium in PDB 6pvc: Structure of Human Mait A-F7 Tcr in Complex with Human MR1-DB28

Protein crystallography data

The structure of Structure of Human Mait A-F7 Tcr in Complex with Human MR1-DB28, PDB code: 6pvc was solved by W.Awad, J.Rossjohn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.42 / 1.96
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 214.291, 69.834, 141.618, 90.00, 103.32, 90.00
R / Rfree (%) 16.9 / 21.2

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of Human Mait A-F7 Tcr in Complex with Human MR1-DB28 (pdb code 6pvc). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structure of Human Mait A-F7 Tcr in Complex with Human MR1-DB28, PDB code: 6pvc:

Sodium binding site 1 out of 1 in 6pvc

Go back to Sodium Binding Sites List in 6pvc
Sodium binding site 1 out of 1 in the Structure of Human Mait A-F7 Tcr in Complex with Human MR1-DB28


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Human Mait A-F7 Tcr in Complex with Human MR1-DB28 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Na101

b:46.2
occ:1.00
O D:LEU87 2.3 37.8 1.0
O D:HOH283 2.4 64.6 1.0
O D:HOH272 2.4 51.1 1.0
OD1 D:ASN83 2.5 46.0 1.0
O D:HIS84 2.6 34.1 1.0
CG D:ASN83 3.4 44.0 1.0
C D:HIS84 3.5 36.0 1.0
C D:LEU87 3.5 40.2 1.0
ND2 D:ASN83 3.9 49.3 1.0
N D:HIS84 3.9 34.8 1.0
CA D:VAL85 4.2 34.7 1.0
N D:VAL85 4.2 34.7 1.0
N D:LEU87 4.2 37.9 1.0
CA D:LEU87 4.2 40.1 1.0
CB D:LEU87 4.3 39.0 1.0
C D:VAL85 4.4 39.8 1.0
O D:VAL85 4.4 36.2 1.0
CA D:HIS84 4.4 35.6 1.0
N D:SER88 4.5 41.0 1.0
O D:HOH295 4.6 52.8 1.0
C D:SER88 4.6 41.4 1.0
CB D:ASN83 4.7 36.6 1.0
CA D:SER88 4.7 43.6 1.0
C D:ASN83 4.8 34.4 1.0
O D:SER88 4.9 43.7 1.0
N D:GLN89 4.9 43.6 1.0
CA D:ASN83 4.9 33.4 1.0

Reference:

W.Awad, J.Rossjohn. Immune Receptor Complex Proc.Natl.Acad.Sci.Usa 2020.
ISSN: ESSN 1091-6490
DOI: 10.1073/PNAS.2003136117
Page generated: Tue Oct 8 12:46:51 2024

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