Magnesium in PDB 1e9i: Enolase From E.Coli
Enzymatic activity of Enolase From E.Coli
All present enzymatic activity of Enolase From E.Coli:
4.2.1.11;
Protein crystallography data
The structure of Enolase From E.Coli, PDB code: 1e9i
was solved by
K.Kuhnel,
A.J.Carpousis,
B.Luisi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
27.97 /
2.48
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
107.883,
150.006,
127.411,
90.00,
109.18,
90.00
|
R / Rfree (%)
|
22.9 /
27.6
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Enolase From E.Coli
(pdb code 1e9i). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the
Enolase From E.Coli, PDB code: 1e9i:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
Magnesium binding site 1 out
of 5 in 1e9i
Go back to
Magnesium Binding Sites List in 1e9i
Magnesium binding site 1 out
of 5 in the Enolase From E.Coli
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Enolase From E.Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1431
b:31.6
occ:1.00
|
O
|
A:HOH2080
|
1.9
|
31.7
|
1.0
|
O
|
A:HOH2095
|
2.0
|
36.9
|
1.0
|
OD2
|
A:ASP316
|
2.0
|
25.1
|
1.0
|
OE2
|
A:GLU289
|
2.1
|
34.4
|
1.0
|
O
|
A:HOH2052
|
2.2
|
40.1
|
1.0
|
OD2
|
A:ASP245
|
2.4
|
32.0
|
1.0
|
CG
|
A:ASP316
|
3.1
|
27.1
|
1.0
|
CG
|
A:ASP245
|
3.3
|
34.5
|
1.0
|
CD
|
A:GLU289
|
3.3
|
30.7
|
1.0
|
OD1
|
A:ASP245
|
3.5
|
35.8
|
1.0
|
CB
|
A:ASP316
|
3.6
|
28.2
|
1.0
|
O
|
A:HOH2054
|
3.8
|
31.3
|
1.0
|
O
|
A:HOH2099
|
3.9
|
49.4
|
1.0
|
NZ
|
A:LYS392
|
4.1
|
33.8
|
1.0
|
OE1
|
A:GLU289
|
4.1
|
31.0
|
1.0
|
OD2
|
A:ASP290
|
4.2
|
33.1
|
1.0
|
OD1
|
A:ASP316
|
4.2
|
24.3
|
1.0
|
CG
|
A:GLU289
|
4.3
|
27.6
|
1.0
|
NE2
|
A:GLN166
|
4.3
|
30.6
|
1.0
|
O
|
A:HOH2015
|
4.4
|
31.6
|
1.0
|
O
|
A:HOH2118
|
4.4
|
30.7
|
1.0
|
CB
|
A:ASP245
|
4.6
|
32.7
|
1.0
|
NZ
|
A:LYS341
|
4.6
|
40.1
|
1.0
|
CD2
|
A:LEU339
|
4.7
|
34.8
|
1.0
|
O
|
A:HOH2050
|
4.9
|
60.4
|
1.0
|
|
Magnesium binding site 2 out
of 5 in 1e9i
Go back to
Magnesium Binding Sites List in 1e9i
Magnesium binding site 2 out
of 5 in the Enolase From E.Coli
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Enolase From E.Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1431
b:42.8
occ:1.00
|
O
|
B:HOH2086
|
2.0
|
40.2
|
1.0
|
OE2
|
B:GLU289
|
2.1
|
59.4
|
1.0
|
O
|
B:HOH2087
|
2.1
|
61.4
|
1.0
|
OD2
|
B:ASP245
|
2.2
|
62.3
|
1.0
|
OD2
|
B:ASP316
|
2.4
|
52.9
|
1.0
|
CD
|
B:GLU289
|
3.2
|
59.3
|
1.0
|
CG
|
B:ASP245
|
3.2
|
66.1
|
1.0
|
CG
|
B:ASP316
|
3.3
|
54.9
|
1.0
|
OD1
|
B:ASP245
|
3.6
|
65.3
|
1.0
|
CB
|
B:ASP316
|
3.6
|
55.8
|
1.0
|
OD2
|
B:ASP290
|
3.8
|
54.0
|
1.0
|
OE1
|
B:GLU289
|
4.0
|
60.9
|
1.0
|
NZ
|
B:LYS392
|
4.0
|
42.2
|
1.0
|
CG
|
B:GLU289
|
4.0
|
59.9
|
1.0
|
NE2
|
B:GLN166
|
4.3
|
66.5
|
1.0
|
O
|
B:HOH2092
|
4.4
|
49.5
|
1.0
|
OD1
|
B:ASP316
|
4.4
|
54.9
|
1.0
|
O
|
B:HOH2080
|
4.5
|
47.8
|
1.0
|
CD2
|
B:LEU339
|
4.5
|
34.2
|
1.0
|
CB
|
B:ASP245
|
4.5
|
68.5
|
1.0
|
CG
|
B:ASP290
|
4.9
|
53.0
|
1.0
|
NZ
|
B:LYS341
|
4.9
|
28.2
|
1.0
|
OE2
|
B:GLU167
|
5.0
|
63.5
|
1.0
|
CB
|
B:GLU289
|
5.0
|
60.1
|
1.0
|
|
Magnesium binding site 3 out
of 5 in 1e9i
Go back to
Magnesium Binding Sites List in 1e9i
Magnesium binding site 3 out
of 5 in the Enolase From E.Coli
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Enolase From E.Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1429
b:68.4
occ:1.00
|
O
|
C:HOH2080
|
1.9
|
44.0
|
1.0
|
O
|
C:HOH2098
|
1.9
|
50.0
|
1.0
|
OE2
|
C:GLU289
|
2.0
|
60.4
|
1.0
|
O
|
C:HOH2077
|
2.4
|
57.6
|
1.0
|
OD2
|
C:ASP316
|
2.8
|
77.3
|
1.0
|
OD2
|
C:ASP245
|
2.9
|
80.2
|
1.0
|
O
|
C:HOH2082
|
3.1
|
44.0
|
1.0
|
CD
|
C:GLU289
|
3.2
|
62.5
|
1.0
|
NZ
|
C:LYS392
|
3.4
|
37.0
|
1.0
|
CG
|
C:ASP316
|
3.4
|
77.0
|
1.0
|
O
|
C:HOH2083
|
3.7
|
49.2
|
1.0
|
CB
|
C:ASP316
|
3.8
|
76.0
|
1.0
|
OE1
|
C:GLU289
|
3.9
|
61.1
|
1.0
|
CG
|
C:ASP245
|
3.9
|
81.4
|
1.0
|
CD2
|
C:LEU339
|
4.1
|
43.5
|
1.0
|
OD2
|
C:ASP290
|
4.1
|
85.5
|
1.0
|
OD1
|
C:ASP245
|
4.2
|
83.7
|
1.0
|
OD1
|
C:ASP316
|
4.3
|
77.7
|
1.0
|
CG
|
C:GLU289
|
4.3
|
63.6
|
1.0
|
OE2
|
C:GLU167
|
4.5
|
70.8
|
1.0
|
CE
|
C:LYS392
|
4.8
|
37.6
|
1.0
|
NZ
|
C:LYS341
|
4.9
|
46.6
|
1.0
|
|
Magnesium binding site 4 out
of 5 in 1e9i
Go back to
Magnesium Binding Sites List in 1e9i
Magnesium binding site 4 out
of 5 in the Enolase From E.Coli
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Enolase From E.Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg1432
b:43.3
occ:1.00
|
O
|
D:HOH2082
|
2.0
|
32.5
|
1.0
|
OE2
|
D:GLU289
|
2.1
|
35.8
|
1.0
|
OD2
|
D:ASP316
|
2.1
|
37.2
|
1.0
|
OD2
|
D:ASP245
|
2.4
|
28.3
|
1.0
|
O
|
D:HOH2114
|
2.5
|
44.7
|
1.0
|
CG
|
D:ASP316
|
3.1
|
38.1
|
1.0
|
CG
|
D:ASP245
|
3.2
|
31.6
|
1.0
|
CD
|
D:GLU289
|
3.2
|
30.0
|
1.0
|
OD1
|
D:ASP245
|
3.4
|
30.6
|
1.0
|
OD2
|
D:ASP290
|
3.4
|
28.3
|
1.0
|
O
|
D:HOH2108
|
3.5
|
31.3
|
1.0
|
MG
|
D:MG1433
|
3.5
|
41.4
|
1.0
|
CB
|
D:ASP316
|
3.6
|
37.2
|
1.0
|
O
|
D:HOH2109
|
3.7
|
35.4
|
1.0
|
NE2
|
D:GLN166
|
4.0
|
41.3
|
1.0
|
CG
|
D:GLU289
|
4.1
|
28.8
|
1.0
|
OE1
|
D:GLU289
|
4.1
|
31.8
|
1.0
|
NZ
|
D:LYS392
|
4.2
|
27.3
|
1.0
|
OD1
|
D:ASP316
|
4.2
|
39.6
|
1.0
|
NZ
|
D:LYS341
|
4.2
|
36.7
|
1.0
|
CD2
|
D:LEU339
|
4.3
|
30.2
|
1.0
|
OE2
|
D:GLU167
|
4.4
|
36.1
|
1.0
|
CG
|
D:ASP290
|
4.6
|
29.2
|
1.0
|
CB
|
D:ASP245
|
4.6
|
33.6
|
1.0
|
OD2
|
D:ASP317
|
4.8
|
33.2
|
1.0
|
O3
|
D:SO41434
|
4.8
|
52.8
|
1.0
|
CB
|
D:ALA247
|
4.8
|
42.8
|
1.0
|
OD1
|
D:ASP317
|
4.9
|
31.9
|
1.0
|
|
Magnesium binding site 5 out
of 5 in 1e9i
Go back to
Magnesium Binding Sites List in 1e9i
Magnesium binding site 5 out
of 5 in the Enolase From E.Coli
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Enolase From E.Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg1433
b:41.4
occ:1.00
|
O
|
D:HOH2109
|
2.0
|
35.4
|
1.0
|
O2
|
D:SO41434
|
2.2
|
47.4
|
1.0
|
O
|
D:HOH2108
|
2.2
|
31.3
|
1.0
|
OG
|
D:SER41
|
2.3
|
49.8
|
1.0
|
O
|
D:SER41
|
2.6
|
54.9
|
1.0
|
S
|
D:SO41434
|
3.3
|
52.0
|
1.0
|
CB
|
D:SER41
|
3.4
|
52.7
|
1.0
|
O3
|
D:SO41434
|
3.4
|
52.8
|
1.0
|
C
|
D:SER41
|
3.5
|
53.4
|
1.0
|
MG
|
D:MG1432
|
3.5
|
43.3
|
1.0
|
OD2
|
D:ASP316
|
3.6
|
37.2
|
1.0
|
O
|
D:HOH2114
|
3.7
|
44.7
|
1.0
|
OD1
|
D:ASP317
|
3.7
|
31.9
|
1.0
|
NZ
|
D:LYS341
|
3.8
|
36.7
|
1.0
|
CA
|
D:SER41
|
4.0
|
53.4
|
1.0
|
O4
|
D:SO41434
|
4.0
|
52.2
|
1.0
|
OD2
|
D:ASP317
|
4.2
|
33.2
|
1.0
|
NE2
|
D:GLN166
|
4.2
|
41.3
|
1.0
|
NH2
|
D:ARG370
|
4.2
|
39.5
|
1.0
|
CG
|
D:ASP317
|
4.4
|
34.3
|
1.0
|
N
|
D:SER41
|
4.4
|
52.1
|
1.0
|
OE1
|
D:GLN166
|
4.4
|
44.1
|
1.0
|
O1
|
D:SO41434
|
4.5
|
47.2
|
1.0
|
N
|
D:THR42
|
4.5
|
53.9
|
1.0
|
O
|
D:HOH2082
|
4.6
|
32.5
|
1.0
|
CG
|
D:ASP316
|
4.6
|
38.1
|
1.0
|
CD
|
D:GLN166
|
4.8
|
42.0
|
1.0
|
CA
|
D:THR42
|
4.9
|
53.3
|
1.0
|
|
Reference:
K.Kuhnel,
B.Luisi.
Crystal Structure of the Escherichia Coli Rna Degradosome Component Enolase J.Mol.Biol. V. 313 583 2001.
ISSN: ISSN 0022-2836
PubMed: 11676541
DOI: 10.1006/JMBI.2001.5065
Page generated: Tue Aug 13 02:53:25 2024
|