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Manganese in PDB 1x7z: Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase

Enzymatic activity of Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase

All present enzymatic activity of Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase:
1.2.4.4;

Protein crystallography data

The structure of Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase, PDB code: 1x7z was solved by R.M.Wynn, M.Kato, M.Machius, J.L.Chuang, J.Li, D.R.Tomchick, D.T.Chuang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.72
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 145.310, 145.310, 69.322, 90.00, 90.00, 120.00
R / Rfree (%) 15.3 / 18.9

Other elements in 1x7z:

The structure of Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase also contains other interesting chemical elements:

Potassium (K) 2 atoms
Chlorine (Cl) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase (pdb code 1x7z). 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 Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase, PDB code: 1x7z:

Manganese binding site 1 out of 1 in 1x7z

Go back to Manganese Binding Sites List in 1x7z
Manganese binding site 1 out of 1 in the Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Human Mitochondrial Branched-Chain Alpha- Ketoacid Dehydrogenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn703

b:13.3
occ:1.00
 O22 A:TDP801 2.1 2.0 1.0
O13 A:TDP801 2.1 2.0 1.0
O A:TYR224 2.2 6.1 1.0
OE1 A:GLU193 2.2 7.8 1.0
OD1 A:ASN222 2.3 8.6 1.0
O A:HOH813 2.4 14.2 1.0
OE2 A:GLU193 2.8 8.1 1.0
CD A:GLU193 2.9 8.4 1.0
CG A:ASN222 3.1 9.6 1.0
C A:TYR224 3.3 6.3 1.0
P1 A:TDP801 3.3 2.0 1.0
P2 A:TDP801 3.3 2.0 1.0
O11 A:TDP801 3.4 2.0 1.0
ND2 A:ASN222 3.5 10.7 1.0
O5G A:TDP801 4.0 2.0 1.0
N A:TYR224 4.0 8.8 1.0
O23 A:TDP801 4.1 2.0 1.0
N A:ALA225 4.1 6.2 1.0
CA A:ALA225 4.2 5.7 1.0
N A:GLU193 4.2 6.6 1.0
CA A:TYR224 4.3 7.4 1.0
N A:ASN222 4.3 8.8 1.0
CG A:GLU193 4.3 5.6 1.0
N A:GLY194 4.5 5.0 1.0
CB A:ASN222 4.5 11.2 1.0
O A:HOH840 4.5 19.0 1.0
O12 A:TDP801 4.5 2.0 1.0
O A:ARG220 4.5 8.2 1.0
O21 A:TDP801 4.5 4.3 1.0
CB A:ALA225 4.7 5.3 1.0
N A:GLY223 4.7 10.2 1.0
C A:ASN222 4.7 11.8 1.0
CA A:ASN222 4.7 9.8 1.0
CA A:GLY192 4.9 6.3 1.0
CA A:GLU193 4.9 6.6 1.0
CB A:GLU193 4.9 5.9 1.0
C A:GLY192 5.0 7.1 1.0
O A:HOH866 5.0 24.2 1.0

Reference:

R.M.Wynn, M.Kato, M.Machius, J.L.Chuang, J.Li, D.R.Tomchick, D.T.Chuang. Molecular Mechanism For Regulation of the Human Mitochondrial Branched-Chain Alpha-Ketoacid Dehydrogenase Complex By Phosphorylation Structure V. 12 2185 2004.
ISSN: ISSN 0969-2126
PubMed: 15576032
DOI: 10.1016/J.STR.2004.09.013
Page generated: Sat Oct 5 13:01:07 2024

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