Magnesium in PDB 1l8a: E. Coli Pyruvate Dehydrogenase
Enzymatic activity of E. Coli Pyruvate Dehydrogenase
All present enzymatic activity of E. Coli Pyruvate Dehydrogenase:
1.2.4.1;
Protein crystallography data
The structure of E. Coli Pyruvate Dehydrogenase, PDB code: 1l8a
was solved by
W.Furey,
P.Arjunan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
8.00 /
1.85
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
81.690,
141.600,
82.460,
90.00,
102.40,
90.00
|
R / Rfree (%)
|
18.9 /
23.6
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the E. Coli Pyruvate Dehydrogenase
(pdb code 1l8a). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the
E. Coli Pyruvate Dehydrogenase, PDB code: 1l8a:
Jump to Magnesium binding site number:
1;
2;
Magnesium binding site 1 out
of 2 in 1l8a
Go back to
Magnesium Binding Sites List in 1l8a
Magnesium binding site 1 out
of 2 in the E. Coli Pyruvate Dehydrogenase
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of E. Coli Pyruvate Dehydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg888
b:13.2
occ:1.00
|
OD1
|
B:ASP230
|
2.1
|
9.8
|
1.0
|
OD1
|
B:ASN260
|
2.1
|
10.3
|
1.0
|
O
|
B:GLN262
|
2.2
|
12.6
|
1.0
|
O
|
B:HOH903
|
2.3
|
12.3
|
1.0
|
O12
|
A:TDP887
|
2.4
|
10.9
|
1.0
|
O23
|
A:TDP887
|
2.5
|
11.1
|
1.0
|
CG
|
B:ASN260
|
3.1
|
10.6
|
1.0
|
CG
|
B:ASP230
|
3.1
|
10.0
|
1.0
|
C
|
B:GLN262
|
3.3
|
15.7
|
1.0
|
ND2
|
B:ASN260
|
3.4
|
9.8
|
1.0
|
P2
|
A:TDP887
|
3.5
|
11.6
|
1.0
|
P1
|
A:TDP887
|
3.6
|
10.1
|
1.0
|
OD2
|
B:ASP230
|
3.6
|
12.2
|
1.0
|
O11
|
A:TDP887
|
3.6
|
11.0
|
1.0
|
N
|
B:GLN262
|
3.8
|
13.6
|
1.0
|
N
|
B:ASP230
|
3.9
|
8.8
|
1.0
|
O21
|
A:TDP887
|
4.0
|
11.9
|
1.0
|
N
|
B:GLY231
|
4.0
|
10.4
|
1.0
|
O
|
B:ASN258
|
4.0
|
10.1
|
1.0
|
CA
|
B:GLN262
|
4.1
|
16.3
|
1.0
|
N
|
B:ARG263
|
4.2
|
14.8
|
1.0
|
CB
|
B:ASP230
|
4.4
|
8.7
|
1.0
|
CA
|
B:ARG263
|
4.4
|
14.9
|
1.0
|
O5G
|
A:TDP887
|
4.4
|
11.5
|
1.0
|
N
|
B:ASN260
|
4.4
|
9.8
|
1.0
|
CB
|
B:ASN260
|
4.4
|
9.5
|
1.0
|
CA
|
B:ASP230
|
4.5
|
8.7
|
1.0
|
N
|
B:LEU261
|
4.6
|
9.4
|
1.0
|
O13
|
A:TDP887
|
4.7
|
10.1
|
1.0
|
C
|
B:ASN260
|
4.8
|
10.0
|
1.0
|
C
|
B:ASP230
|
4.8
|
7.8
|
1.0
|
CA
|
B:ASN260
|
4.8
|
9.6
|
1.0
|
NZ
|
B:LYS392
|
4.8
|
30.3
|
1.0
|
C
|
B:GLY229
|
4.8
|
9.9
|
1.0
|
C
|
B:LEU261
|
4.8
|
12.4
|
1.0
|
O22
|
A:TDP887
|
4.8
|
14.5
|
1.0
|
CB
|
B:GLN262
|
4.9
|
22.8
|
1.0
|
CG2
|
B:VAL268
|
4.9
|
14.4
|
1.0
|
CA
|
B:GLY229
|
4.9
|
8.6
|
1.0
|
CE
|
B:LYS392
|
4.9
|
32.3
|
1.0
|
CA
|
B:GLY231
|
4.9
|
8.9
|
1.0
|
|
Magnesium binding site 2 out
of 2 in 1l8a
Go back to
Magnesium Binding Sites List in 1l8a
Magnesium binding site 2 out
of 2 in the E. Coli Pyruvate Dehydrogenase
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of E. Coli Pyruvate Dehydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg888
b:13.2
occ:1.00
|
OD1
|
A:ASN260
|
2.1
|
8.6
|
1.0
|
OD2
|
A:ASP230
|
2.2
|
14.4
|
1.0
|
O
|
A:GLN262
|
2.3
|
15.2
|
1.0
|
O
|
A:HOH909
|
2.3
|
8.0
|
1.0
|
O23
|
B:TDP887
|
2.5
|
16.0
|
1.0
|
O12
|
B:TDP887
|
2.5
|
14.1
|
1.0
|
CG
|
A:ASN260
|
3.0
|
12.0
|
1.0
|
CG
|
A:ASP230
|
3.2
|
15.6
|
1.0
|
ND2
|
A:ASN260
|
3.4
|
10.2
|
1.0
|
C
|
A:GLN262
|
3.4
|
18.4
|
1.0
|
P2
|
B:TDP887
|
3.5
|
16.7
|
1.0
|
OD1
|
A:ASP230
|
3.6
|
11.2
|
1.0
|
O11
|
B:TDP887
|
3.6
|
13.4
|
1.0
|
P1
|
B:TDP887
|
3.6
|
13.3
|
1.0
|
O
|
A:ASN258
|
3.8
|
10.2
|
1.0
|
N
|
A:ASP230
|
3.8
|
8.2
|
1.0
|
O21
|
B:TDP887
|
3.9
|
16.1
|
1.0
|
N
|
A:GLN262
|
3.9
|
17.2
|
1.0
|
N
|
A:GLY231
|
4.1
|
9.1
|
1.0
|
CA
|
A:GLN262
|
4.2
|
20.1
|
1.0
|
N
|
A:ASN260
|
4.2
|
11.4
|
1.0
|
CB
|
A:ASN260
|
4.4
|
10.7
|
1.0
|
CB
|
A:ASP230
|
4.4
|
11.2
|
1.0
|
O5G
|
B:TDP887
|
4.4
|
15.7
|
1.0
|
N
|
A:ARG263
|
4.5
|
16.9
|
1.0
|
N
|
A:LEU261
|
4.5
|
11.5
|
1.0
|
CA
|
A:ASP230
|
4.5
|
8.9
|
1.0
|
CA
|
A:ARG263
|
4.6
|
16.4
|
1.0
|
CA
|
A:ASN260
|
4.7
|
12.4
|
1.0
|
C
|
A:GLY229
|
4.7
|
8.4
|
1.0
|
CA
|
A:GLY229
|
4.7
|
7.6
|
1.0
|
CD
|
A:LYS392
|
4.7
|
33.7
|
1.0
|
C
|
A:ASN260
|
4.7
|
12.2
|
1.0
|
O13
|
B:TDP887
|
4.8
|
11.8
|
1.0
|
O22
|
B:TDP887
|
4.8
|
17.6
|
1.0
|
C
|
A:ASP230
|
4.9
|
9.2
|
1.0
|
C
|
A:LEU261
|
4.9
|
16.0
|
1.0
|
CB
|
A:GLN262
|
5.0
|
23.7
|
1.0
|
|
Reference:
P.Arjunan,
N.Nemeria,
A.Brunskill,
K.Chandrasekhar,
M.Sax,
Y.Yan,
F.Jordan,
J.R.Guest,
W.Furey.
Structure of the Pyruvate Dehydrogenase Multienzyme Complex E1 Component From Escherichia Coli at 1.85 A Resolution. Biochemistry V. 41 5213 2002.
ISSN: ISSN 0006-2960
PubMed: 11955070
DOI: 10.1021/BI0118557
Page generated: Tue Aug 13 08:26:56 2024
|