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Chlorine in PDB 2bfe: Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch

Enzymatic activity of Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch

All present enzymatic activity of Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch:
1.2.4.4;

Protein crystallography data

The structure of Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch, PDB code: 2bfe was solved by M.Machius, R.M.Wynn, J.L.Chuang, D.R.Tomchick, C.A.Brautigam, D.T.Chuang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.69
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 145.181, 145.181, 69.573, 90.00, 90.00, 120.00
R / Rfree (%) 15 / 18.1

Other elements in 2bfe:

The structure of Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch also contains other interesting chemical elements:

Potassium (K) 2 atoms
Manganese (Mn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch (pdb code 2bfe). 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 Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch, PDB code: 2bfe:

Chlorine binding site 1 out of 1 in 2bfe

Go back to Chlorine Binding Sites List in 2bfe
Chlorine binding site 1 out of 1 in the Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl504

b:67.4
occ:1.00
 O A:HOH2177 3.2 33.6 1.0
O A:HOH2115 3.3 31.6 1.0
CE1 A:HIS149 3.4 15.8 0.3
CE1 A:HIS149 3.5 11.2 0.3
NE2 A:HIS149 3.6 12.1 0.3
CE A:MET87 3.7 30.5 0.5
NE2 A:HIS149 4.0 18.6 0.3
O A:HOH2257 4.2 57.6 1.0
SD A:MET87 4.3 23.4 0.5
NE2 A:HIS149 4.3 10.7 0.3
CB A:ALA113 4.4 24.7 0.5
SD A:MET87 4.5 35.8 0.5
ND1 A:HIS149 4.5 19.0 0.3
CB A:SER162 4.6 16.6 1.0
CA A:SER162 4.7 15.5 1.0
ND1 A:HIS149 4.7 15.6 0.3
CE1 A:HIS149 4.7 8.2 0.3
OG A:SER162 4.8 27.8 1.0
CZ A:PHE85 4.8 23.1 1.0
C2 A:TDP601 4.9 12.4 1.0
CD2 A:HIS149 4.9 12.1 0.3
CE2 A:PHE85 5.0 24.2 1.0

Reference:

M.Machius, R.M.Wynn, J.L.Chuang, J.Li, R.Kluger, D.Yu, D.R.Tomchick, C.A.Brautigam, D.T.Chuang. A Versatile Conformational Switch Regulates Reactivity in Human Branched-Chain Alpha-Ketoacid Dehydrogenase. Structure V. 14 287 2006.
ISSN: ISSN 0969-2126
PubMed: 16472748
DOI: 10.1016/J.STR.2005.10.009
Page generated: Sat Jul 20 05:41:22 2024

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