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Chlorine in PDB 4azv: Co-Crystal Structure of Wbdd and Kinase Inhibitor GW435821X.

Protein crystallography data

The structure of Co-Crystal Structure of Wbdd and Kinase Inhibitor GW435821X., PDB code: 4azv was solved by G.Hagelueken, H.Huang, J.H.Naismith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 112.656 / 3.29
Space group I 2 3
Cell size a, b, c (Å), α, β, γ (°) 159.320, 159.320, 159.320, 90.00, 90.00, 90.00
R / Rfree (%) 22.25 / 26.53

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Co-Crystal Structure of Wbdd and Kinase Inhibitor GW435821X. (pdb code 4azv). 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 Co-Crystal Structure of Wbdd and Kinase Inhibitor GW435821X., PDB code: 4azv:

Chlorine binding site 1 out of 1 in 4azv

Go back to Chlorine Binding Sites List in 4azv
Chlorine binding site 1 out of 1 in the Co-Crystal Structure of Wbdd and Kinase Inhibitor GW435821X.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Co-Crystal Structure of Wbdd and Kinase Inhibitor GW435821X. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1479

b:85.9
occ:1.00
H A:ALA162 2.4 0.8 1.0
HD1 A:HIS132 2.4 0.9 1.0
H A:HIS132 2.5 0.5 1.0
HA A:LEU161 2.6 0.0 1.0
HA A:SER129 2.9 0.7 1.0
H A:PHE131 3.1 0.6 1.0
HB3 A:HIS132 3.2 0.2 1.0
N A:ALA162 3.2 66.7 1.0
HD21 A:LEU161 3.2 0.6 1.0
ND1 A:HIS132 3.2 90.9 1.0
N A:HIS132 3.3 78.3 1.0
H A:VAL130 3.3 0.1 1.0
O A:GLU160 3.4 63.2 1.0
CA A:LEU161 3.5 67.8 1.0
N A:PHE131 3.6 78.8 1.0
HB2 A:PHE131 3.6 0.1 1.0
N A:VAL130 3.6 80.0 1.0
CA A:SER129 3.7 63.3 1.0
HB1 A:ALA162 3.7 0.6 1.0
H A:SER129 3.8 0.7 1.0
CB A:HIS132 3.8 85.2 1.0
C A:SER129 3.9 65.8 1.0
HB3 A:ALA162 3.9 0.6 1.0
C A:LEU161 3.9 67.9 1.0
HD23 A:LEU161 4.0 0.6 1.0
CG A:HIS132 4.0 88.0 1.0
CD2 A:LEU161 4.0 67.0 1.0
CA A:PHE131 4.1 79.2 1.0
CA A:HIS132 4.1 81.0 1.0
C A:PHE131 4.1 79.8 1.0
CB A:ALA162 4.1 60.7 1.0
N A:SER129 4.1 62.3 1.0
C A:VAL130 4.2 79.7 1.0
CA A:ALA162 4.2 66.5 1.0
HB3 A:LEU161 4.3 0.1 1.0
CB A:PHE131 4.3 68.1 1.0
CE1 A:HIS132 4.3 91.5 1.0
C A:GLU160 4.3 62.5 1.0
CB A:LEU161 4.4 66.5 1.0
N A:LEU161 4.4 65.2 1.0
HA A:HIS132 4.5 0.2 1.0
HE1 A:HIS132 4.5 0.5 1.0
CA A:VAL130 4.5 79.2 1.0
HD22 A:LEU161 4.7 0.6 1.0
HB2 A:HIS132 4.7 0.2 1.0
O A:SER129 4.7 63.8 1.0
HB3 A:PHE131 4.8 0.1 1.0
CG A:LEU161 4.8 66.4 1.0
CB A:SER129 4.9 52.6 1.0
HA A:ALA162 4.9 0.6 1.0
HD2 A:PHE131 4.9 0.5 1.0
HD3 A:ARG203 4.9 0.0 1.0
HA A:VAL130 4.9 0.3 1.0

Reference:

G.Hagelueken, H.Huang, B.R.Clarke, T.Lebl, C.Whitfield, J.H.Naismith. Structure of Wbdd; A Bifunctional Kinase and Methyltransferase That Regulates the Chain Length of the O Antigen in Escherichia Coli O9A. Mol.Microbiol. V. 86 730 2012.
ISSN: ISSN 0950-382X
PubMed: 22970759
DOI: 10.1111/MMI.12014
Page generated: Sun Jul 21 09:33:58 2024

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