Atomistry » Manganese » PDB 1w2c-1xie » 1x7y
Atomistry »
  Manganese »
    PDB 1w2c-1xie »
      1x7y »

Manganese in PDB 1x7y: 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: 1x7y 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 / 1.57
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 145.672, 145.672, 69.236, 90.00, 90.00, 120.00
R / Rfree (%) 15 / 16.7

Other elements in 1x7y:

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 1x7y). 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: 1x7y:

Manganese binding site 1 out of 1 in 1x7y

Go back to Manganese Binding Sites List in 1x7y
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:Mn803

b:12.5
occ:1.00
 O22 A:TDP901 2.1 2.0 1.0
O A:TYR224 2.1 6.1 1.0
O13 A:TDP901 2.2 2.0 1.0
OE1 A:GLU193 2.2 6.7 1.0
OD1 A:ASN222 2.2 7.4 1.0
O A:HOH915 2.3 13.5 1.0
OE2 A:GLU193 2.8 8.1 1.0
CD A:GLU193 2.9 5.9 1.0
CG A:ASN222 3.2 9.1 1.0
C A:TYR224 3.2 5.5 1.0
P1 A:TDP901 3.3 2.0 1.0
P2 A:TDP901 3.3 2.0 1.0
O11 A:TDP901 3.5 2.0 1.0
ND2 A:ASN222 3.6 10.3 1.0
N A:TYR224 4.0 6.3 1.0
O5G A:TDP901 4.1 2.0 1.0
N A:ALA225 4.1 5.4 1.0
O A:HOH1032 4.1 30.7 1.0
O23 A:TDP901 4.1 2.4 1.0
N A:ASN222 4.2 8.4 1.0
N A:GLU193 4.2 4.8 1.0
CA A:TYR224 4.2 6.7 1.0
CA A:ALA225 4.2 5.7 1.0
CG A:GLU193 4.3 5.0 1.0
N A:GLY194 4.5 5.0 1.0
O A:ARG220 4.5 8.0 1.0
O21 A:TDP901 4.5 2.0 1.0
CB A:ASN222 4.5 10.1 1.0
O12 A:TDP901 4.6 2.0 1.0
O A:HOH957 4.6 20.5 1.0
CB A:ALA225 4.7 6.3 1.0
CA A:ASN222 4.7 8.9 1.0
N A:GLY223 4.8 7.8 1.0
C A:ASN222 4.8 9.0 1.0
CA A:GLY192 4.9 4.4 1.0
CB A:GLU193 5.0 5.0 1.0
O A:HOH965 5.0 22.6 1.0
C A:GLY192 5.0 5.5 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 13:00:57 2024

Last articles

Cl in 2QEE
Cl in 2QG4
Cl in 2QHF
Cl in 2QGW
Cl in 2QF7
Cl in 2QA4
Cl in 2QEI
Cl in 2QEP
Cl in 2QE5
Cl in 2QE3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy