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Chlorine in PDB 2y8f: Structure of the Ran-Binding Domain From Human RANBP3 (Wild Type)

Protein crystallography data

The structure of Structure of the Ran-Binding Domain From Human RANBP3 (Wild Type), PDB code: 2y8f was solved by K.Langer, C.Dian, V.Rybin, C.W.Muller, C.Petosa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.399 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.902, 73.406, 120.410, 90.00, 90.00, 90.00
R / Rfree (%) 19.14 / 22.36

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Ran-Binding Domain From Human RANBP3 (Wild Type) (pdb code 2y8f). 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 Structure of the Ran-Binding Domain From Human RANBP3 (Wild Type), PDB code: 2y8f:

Chlorine binding site 1 out of 1 in 2y8f

Go back to Chlorine Binding Sites List in 2y8f
Chlorine binding site 1 out of 1 in the Structure of the Ran-Binding Domain From Human RANBP3 (Wild Type)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Ran-Binding Domain From Human RANBP3 (Wild Type) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1449

b:51.8
occ:1.00
O A:HOH2037 3.2 38.0 1.0
CG A:LYS390 3.4 22.8 1.0
N A:LYS390 3.4 16.7 1.0
CB A:MET410 3.4 26.6 1.0
CG A:MET410 3.6 29.7 1.0
NH2 A:ARG374 3.8 25.3 1.0
CB A:LYS390 4.0 21.5 1.0
CD A:LYS390 4.0 29.4 1.0
CA A:THR389 4.0 17.1 1.0
OG1 A:THR389 4.1 19.3 1.0
CE A:LYS390 4.2 37.2 1.0
C A:THR389 4.2 18.5 1.0
CA A:LYS390 4.3 19.4 1.0
O A:ASN388 4.4 21.5 1.0
NH1 A:ARG374 4.4 27.6 1.0
CZ A:ARG374 4.5 27.2 1.0
CB A:THR389 4.6 15.3 1.0
CA A:MET410 4.8 22.8 1.0
O A:LYS390 5.0 16.7 1.0

Reference:

K.Langer, C.Dian, V.Rybin, C.W.Muller, C.Petosa. Insights Into the Function of the CRM1 Cofactor RANBP3 From the Structure of Its Ran-Binding Domain Plos One V. 6 17011 2011.
ISSN: ISSN 1932-6203
PubMed: 21364925
DOI: 10.1371/JOURNAL.PONE.0017011
Page generated: Fri Jul 11 02:32:45 2025

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