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Chlorine in PDB 3e8y: Xray Structure of Scorpion Toxin BMBKTX1

Protein crystallography data

The structure of Xray Structure of Scorpion Toxin BMBKTX1, PDB code: 3e8y was solved by K.Mandal, B.L.Pentelute, V.Tereshko, A.A.Kossiakoff, S.B.H.Kent, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.10
Space group I 41/A
Cell size a, b, c (Å), α, β, γ (°) 56.633, 56.633, 31.759, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 21.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Xray Structure of Scorpion Toxin BMBKTX1 (pdb code 3e8y). 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 Xray Structure of Scorpion Toxin BMBKTX1, PDB code: 3e8y:

Chlorine binding site 1 out of 1 in 3e8y

Go back to Chlorine Binding Sites List in 3e8y
Chlorine binding site 1 out of 1 in the Xray Structure of Scorpion Toxin BMBKTX1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Xray Structure of Scorpion Toxin BMBKTX1 within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Cl101

b:9.0
occ:0.50
O X:HOH107 3.0 12.6 1.0
N X:SER25 3.2 10.4 1.0
CA X:SER25 3.8 12.1 0.3
N X:ASN24 3.8 10.0 1.0
CA X:SER25 3.8 11.8 0.3
CA X:SER25 3.8 11.3 0.3
CB X:CYS22 3.9 11.3 1.0
C X:CYS22 4.2 10.6 1.0
C X:ILE23 4.3 9.6 1.0
C X:ASN24 4.3 10.3 1.0
N X:ILE23 4.3 9.5 1.0
O X:CYS22 4.3 13.4 1.0
CA X:ASN24 4.3 11.1 1.0
CA X:ILE23 4.5 10.3 1.0
CA X:CYS22 4.7 10.6 1.0
OG X:SER25 4.7 12.5 0.3
CB X:CYS3 4.7 12.1 1.0
CB X:SER25 4.8 13.8 0.3
C X:SER25 4.8 11.4 1.0
CB X:SER25 4.8 13.8 0.3
CB X:SER25 4.9 13.1 0.3
O X:ILE23 4.9 10.1 1.0
N X:LYS26 5.0 10.2 1.0
O X:CYS3 5.0 11.7 1.0

Reference:

K.Mandal, B.L.Pentelute, V.Tereshko, A.A.Kossiakoff, S.B.Kent. X-Ray Structure of Native Scorpion Toxin BMBKTX1 By Racemic Protein Crystallography Using Direct Methods. J.Am.Chem.Soc. V. 131 1362 2009.
ISSN: ISSN 0002-7863
PubMed: 19133782
DOI: 10.1021/JA8077973
Page generated: Sat Jul 20 18:43:16 2024

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