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Manganese in PDB 2bff: 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: 2bff 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 / 1.46
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 145.133, 145.133, 69.360, 90.00, 90.00, 120.00
R / Rfree (%) 14.9 / 16.6

Other elements in 2bff:

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 Binding Sites:

The binding sites of Manganese atom in the Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch (pdb code 2bff). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Reactivity Modulation of Human Branched-Chain Alpha-Ketoacid Dehydrogenase By An Internal Molecular Switch, PDB code: 2bff:

Manganese binding site 1 out of 1 in 2bff

Go back to Manganese Binding Sites List in 2bff
Manganese 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 Manganese with other atoms in the Mn 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:Mn1402

b:5.3
occ:1.00
 O12 A:TZD601 2.1 2.4 1.0
O A:TYR224 2.2 6.1 1.0
OD1 A:ASN222 2.2 8.1 1.0
OE1 A:GLU193 2.3 7.4 1.0
O22 A:TZD601 2.3 4.0 1.0
O A:HOH2386 2.4 8.7 1.0
OE2 A:GLU193 2.7 7.7 1.0
CD A:GLU193 2.8 6.6 1.0
CG A:ASN222 3.2 11.4 1.0
C A:TYR224 3.2 6.9 1.0
P1 A:TZD601 3.3 4.3 1.0
P2 A:TZD601 3.4 4.7 1.0
ND2 A:ASN222 3.5 12.7 1.0
O11 A:TZD601 3.5 4.8 1.0
N A:TYR224 4.0 9.2 1.0
N A:ALA225 4.1 5.4 1.0
O5G A:TZD601 4.1 4.1 1.0
CA A:ALA225 4.2 4.2 1.0
O23 A:TZD601 4.2 4.6 1.0
N A:ASN222 4.2 8.0 1.0
CA A:TYR224 4.2 7.1 1.0
N A:GLU193 4.2 5.3 1.0
CG A:GLU193 4.3 6.2 1.0
CB A:ASN222 4.4 11.4 1.0
N A:GLY194 4.5 6.5 1.0
O13 A:TZD601 4.5 4.5 1.0
O A:ARG220 4.6 8.4 1.0
O A:HOH2236 4.6 9.2 1.0
O21 A:TZD601 4.6 6.5 1.0
CB A:ALA225 4.6 6.7 1.0
CA A:ASN222 4.6 9.4 1.0
C A:ASN222 4.6 11.7 1.0
N A:GLY223 4.7 10.5 1.0
CA A:GLY192 4.9 6.0 1.0
CB A:GLU193 5.0 5.8 1.0
C A:GLY192 5.0 5.5 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 Oct 5 13:34:22 2024

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