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Sodium in PDB 4h88: Structure of POM1 Fab Fragment Complexed with Mouse Prpc Fragment 120- 230

Protein crystallography data

The structure of Structure of POM1 Fab Fragment Complexed with Mouse Prpc Fragment 120- 230, PDB code: 4h88 was solved by P.K.Baral, B.Wieland, M.Swayampakula, M.N.James, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.01 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 83.406, 107.331, 75.443, 90.00, 95.27, 90.00
R / Rfree (%) 19.9 / 23.4

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of POM1 Fab Fragment Complexed with Mouse Prpc Fragment 120- 230 (pdb code 4h88). 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 POM1 Fab Fragment Complexed with Mouse Prpc Fragment 120- 230, PDB code: 4h88:

Sodium binding site 1 out of 1 in 4h88

Go back to Sodium Binding Sites List in 4h88
Sodium binding site 1 out of 1 in the Structure of POM1 Fab Fragment Complexed with Mouse Prpc Fragment 120- 230


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of POM1 Fab Fragment Complexed with Mouse Prpc Fragment 120- 230 within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Na301

b:12.9
occ:1.00
OE1 L:GLU79 2.6 52.4 1.0
OE1 L:GLU81 2.9 48.0 1.0
OE2 L:GLU81 3.0 51.9 1.0
CD L:GLU81 3.3 47.6 1.0
CD L:GLU79 3.6 46.1 1.0
OE2 L:GLU79 3.9 44.3 1.0
NH1 L:ARG61 4.4 36.5 1.0
NH2 L:ARG61 4.4 38.8 1.0
CZ L:ARG61 4.8 38.8 1.0
CG L:GLU81 4.8 43.6 1.0
CG L:GLU79 5.0 42.6 1.0

Reference:

T.Sonati, R.R.Reimann, J.Falsig, P.K.Baral, T.O'connor, S.Hornemann, S.Yaganoglu, B.Li, U.S.Herrmann, B.Wieland, M.Swayampakula, M.H.Rahman, D.Das, N.Kav, R.Riek, P.P.Liberski, M.N.James, A.Aguzzi. The Toxicity of Antiprion Antibodies Is Mediated By the Flexible Tail of the Prion Protein. Nature V. 501 102 2013.
ISSN: ISSN 0028-0836
PubMed: 23903654
DOI: 10.1038/NATURE12402
Page generated: Mon Oct 7 15:45:11 2024

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