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Sodium in PDB 8ojt: Crystal Structure of the Human Igd Fab - Structure FAB2

Protein crystallography data

The structure of Crystal Structure of the Human Igd Fab - Structure FAB2, PDB code: 8ojt was solved by A.M.Davies, R.L.Beavil, J.M.Mcdonnell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 70.39 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 43.149, 73.827, 70.458, 90, 92.54, 90
R / Rfree (%) 16.1 / 19.8

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Human Igd Fab - Structure FAB2 (pdb code 8ojt). 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 Crystal Structure of the Human Igd Fab - Structure FAB2, PDB code: 8ojt:

Sodium binding site 1 out of 1 in 8ojt

Go back to Sodium Binding Sites List in 8ojt
Sodium binding site 1 out of 1 in the Crystal Structure of the Human Igd Fab - Structure FAB2


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the Human Igd Fab - Structure FAB2 within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Na302

b:44.4
occ:1.00
O2 L:NO3301 2.6 75.0 1.0
OD2 H:ASP109 2.6 26.4 1.0
O L:HOH533 2.8 51.7 1.0
O1 L:NO3301 2.9 75.6 1.0
N L:NO3301 3.1 75.3 1.0
CG H:ASP109 3.6 20.5 1.0
CB H:ASP109 3.7 17.3 1.0
CD2 H:PHE100 3.9 36.9 1.0
CE2 H:PHE100 3.9 38.7 1.0
O H:HOH557 4.0 43.1 1.0
CG H:PHE100 4.0 33.3 1.0
CE H:MET107 4.0 32.5 1.0
CZ H:PHE100 4.0 37.8 1.0
CD1 H:PHE100 4.1 36.3 1.0
CE1 H:PHE100 4.1 37.5 1.0
O3 L:NO3301 4.3 74.8 1.0
O L:HOH453 4.3 27.1 1.0
O H:HOH504 4.3 23.4 1.0
NH2 H:ARG98 4.5 23.0 1.0
O H:HOH465 4.5 32.1 1.0
CB H:PHE100 4.7 26.6 1.0
OD1 H:ASP109 4.7 17.7 1.0

Reference:

A.M.Davies, R.L.Beavil, M.Barbolov, B.S.Sandhar, H.J.Gould, A.J.Beavil, B.J.Sutton, J.M.Mcdonnell. Crystal Structures of the Human Igd Fab Reveal Insights Into C H 1 Domain Diversity. Mol.Immunol. V. 159 28 2023.
ISSN: ISSN 0161-5890
PubMed: 37267832
DOI: 10.1016/J.MOLIMM.2023.05.006
Page generated: Mon Aug 18 14:52:32 2025

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