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Chlorine in PDB 5y9y: Crystal Structure of the Kdo Hydroxylase Kdoo, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Succinate and Co(II)

Protein crystallography data

The structure of Crystal Structure of the Kdo Hydroxylase Kdoo, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Succinate and Co(II), PDB code: 5y9y was solved by H.S.Chung, C.W.Pemble, S.H.Joo, C.R.Raetz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.57 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.762, 59.316, 116.429, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 19.4

Other elements in 5y9y:

The structure of Crystal Structure of the Kdo Hydroxylase Kdoo, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Succinate and Co(II) also contains other interesting chemical elements:

Cobalt (Co) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Kdo Hydroxylase Kdoo, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Succinate and Co(II) (pdb code 5y9y). 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 Crystal Structure of the Kdo Hydroxylase Kdoo, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Succinate and Co(II), PDB code: 5y9y:

Chlorine binding site 1 out of 1 in 5y9y

Go back to Chlorine Binding Sites List in 5y9y
Chlorine binding site 1 out of 1 in the Crystal Structure of the Kdo Hydroxylase Kdoo, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Succinate and Co(II)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Kdo Hydroxylase Kdoo, A Non-Heme Fe(II) Alphaketoglutarate Dependent Dioxygenase in Complex with Succinate and Co(II) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl415

b:28.2
occ:0.75
O A:HOH501 2.7 53.7 1.0
O A:HOH709 2.8 39.0 1.0
O A:HOH663 3.0 21.1 1.0
N A:ASP17 3.2 18.6 1.0
NZ A:LYS32 3.5 61.2 1.0
CA A:PHE16 3.6 18.6 1.0
CD1 A:ILE29 3.8 31.1 1.0
CD2 A:PHE16 3.9 18.1 1.0
C A:PHE16 3.9 19.4 1.0
CB A:PHE16 4.0 15.3 1.0
CB A:ASP17 4.0 24.3 1.0
O A:HOH708 4.1 42.3 1.0
CA A:ASP17 4.2 20.0 1.0
CG1 A:ILE29 4.3 28.5 1.0
CG2 A:ILE29 4.3 22.4 1.0
CG A:ASP17 4.3 41.9 1.0
CG A:PHE16 4.3 14.9 1.0
OD1 A:ASP17 4.3 52.9 1.0
CE A:LYS32 4.4 50.0 1.0
O A:GLN15 4.6 22.8 1.0
O A:HOH728 4.8 26.8 1.0
CE2 A:PHE16 4.8 21.5 1.0
N A:PHE16 4.9 14.8 1.0
N A:ALA18 4.9 17.5 1.0
OD2 A:ASP17 5.0 50.5 1.0
CB A:ILE29 5.0 18.8 1.0

Reference:

H.S.Chung, C.W.Pemble Iv, S.H.Joo. Biochemical and Structural Insights of Fe(II)/Alpha-Ketoglutarate/O2-Dependent Dioxygenase, Kdoo From Methylacidiphilum Infernorum V4 To Be Published.
Page generated: Fri Jul 26 21:21:34 2024

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