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Chlorine in PDB 4lhj: Ricin A Chain Bound to Camelid Nanobody (VHH5)

Enzymatic activity of Ricin A Chain Bound to Camelid Nanobody (VHH5)

All present enzymatic activity of Ricin A Chain Bound to Camelid Nanobody (VHH5):
3.2.2.22;

Protein crystallography data

The structure of Ricin A Chain Bound to Camelid Nanobody (VHH5), PDB code: 4lhj was solved by M.J.Rudolph, J.Cheung, M.Franklin, F.Burshteyn, M.Cassidy, E.Gary, N.Mantis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.71 / 1.80
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 81.419, 103.782, 42.086, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 25

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Ricin A Chain Bound to Camelid Nanobody (VHH5) (pdb code 4lhj). 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 Ricin A Chain Bound to Camelid Nanobody (VHH5), PDB code: 4lhj:

Chlorine binding site 1 out of 1 in 4lhj

Go back to Chlorine Binding Sites List in 4lhj
Chlorine binding site 1 out of 1 in the Ricin A Chain Bound to Camelid Nanobody (VHH5)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Ricin A Chain Bound to Camelid Nanobody (VHH5) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:58.6
occ:1.00
N A:GLY121 3.2 27.8 1.0
CD A:ARG126 3.7 43.1 1.0
CG A:ARG126 3.9 37.7 1.0
CA A:GLY121 3.9 27.1 1.0
CA A:PHE120 4.0 33.0 1.0
NE A:ARG126 4.1 45.6 1.0
C A:PHE120 4.1 29.5 1.0
ND2 A:ASN123 4.3 38.2 1.0
CB A:ARG126 4.4 28.1 1.0
CB A:PHE120 4.4 29.4 1.0
O A:GLY121 4.8 26.4 1.0
C A:GLY121 4.8 26.4 1.0

Reference:

M.J.Rudolph, D.J.Vance, J.Cheung, M.C.Franklin, F.Burshteyn, M.S.Cassidy, E.N.Gary, C.Herrera, C.B.Shoemaker, N.J.Mantis. Crystal Structures of Ricin Toxin'S Enzymatic Subunit (Rta) in Complex with Neutralizing and Non-Neutralizing Single-Chain Antibodies. J.Mol.Biol. V. 426 3057 2014.
ISSN: ISSN 0022-2836
PubMed: 24907552
DOI: 10.1016/J.JMB.2014.05.026
Page generated: Fri Jul 11 18:34:20 2025

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