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Potassium in PDB 8vbj: Structure of Bovine Anti-Hiv Fab ELSE2

Protein crystallography data

The structure of Structure of Bovine Anti-Hiv Fab ELSE2, PDB code: 8vbj was solved by R.L.Stanfield, I.A.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.48 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 69.959, 178.585, 105.706, 90, 90, 90
R / Rfree (%) 19.2 / 23.1

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Bovine Anti-Hiv Fab ELSE2 (pdb code 8vbj). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Structure of Bovine Anti-Hiv Fab ELSE2, PDB code: 8vbj:

Potassium binding site 1 out of 1 in 8vbj

Go back to Potassium Binding Sites List in 8vbj
Potassium binding site 1 out of 1 in the Structure of Bovine Anti-Hiv Fab ELSE2


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Bovine Anti-Hiv Fab ELSE2 within 5.0Å range:
probe atom residue distance (Å) B Occ
H:K301

b:79.0
occ:1.00
O H:HOH520 2.6 42.9 1.0
O L:HOH458 2.7 41.9 1.0
O L:HOH316 2.8 32.8 1.0
O H:HOH438 3.0 43.6 1.0
HB2 H:ASP140 3.3 46.5 1.0
O H:ASP140 3.5 31.7 1.0
H H:ASP140 3.8 45.9 1.0
CB H:ASP140 4.1 38.8 1.0
HB3 H:ASP140 4.1 46.5 1.0
HE2 H:HIS142 4.3 42.9 1.0
O L:HOH423 4.4 35.2 1.0
C H:ASP140 4.4 34.0 1.0
N H:ASP140 4.4 38.2 1.0
CA H:ASP140 4.6 35.5 1.0
HG23 H:ILE139 4.8 47.6 1.0
NE2 H:HIS142 4.8 35.7 1.0
HD2 H:HIS142 4.9 39.5 1.0

Reference:

P.Altman, G.Ozorowski, R.L.Stanfield, J.Haakenson, M.Appel, M.Parren, W.-H.Lee, J.Woehl, K.Saye-Francisco, C.Joyce, G.Song, K.Porter, E.Landais, R.Andrabi, I.A.Wilson, A.B.Ward, W.Mwangi, V.V.Smider, D.R.Burton, D.Sok. Immunization of Cows with Hiv Envelope Trimers Generates Broadly Neutralizing Antibodies to the V2-Apex From the Ultra-Long CDRH3 Repertoire To Be Published.
Page generated: Sat Aug 9 18:09:31 2025

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