Calcium in PDB 1tah: The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate
Enzymatic activity of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate
All present enzymatic activity of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate:
3.1.1.3;
Protein crystallography data
The structure of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate, PDB code: 1tah
was solved by
M.E.M.Noble,
A.Cleasby,
L.N.Johnson,
M.Egmond,
L.G.J.Frenken,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
6.00 /
3.00
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
158.160,
158.640,
63.360,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
15.9 /
22.6
|
Calcium Binding Sites:
The binding sites of Calcium atom in the The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate
(pdb code 1tah). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the
The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate, PDB code: 1tah:
Jump to Calcium binding site number:
1;
2;
3;
4;
Calcium binding site 1 out
of 4 in 1tah
Go back to
Calcium Binding Sites List in 1tah
Calcium binding site 1 out
of 4 in the The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate
 Mono view
 Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca320
b:11.9
occ:1.00
|
OD2
|
B:ASP241
|
2.3
|
33.5
|
1.0
|
OD1
|
B:ASP287
|
2.5
|
72.6
|
1.0
|
O
|
B:VAL295
|
2.6
|
26.5
|
1.0
|
O
|
B:GLN291
|
2.6
|
7.0
|
1.0
|
CG
|
B:ASP241
|
3.4
|
22.4
|
1.0
|
CG
|
B:ASP287
|
3.7
|
4.8
|
1.0
|
C
|
B:VAL295
|
3.7
|
5.2
|
1.0
|
C
|
B:GLN291
|
3.8
|
17.4
|
1.0
|
OG
|
B:SER243
|
4.0
|
20.1
|
1.0
|
OD1
|
B:ASP241
|
4.1
|
18.6
|
1.0
|
OD1
|
B:ASN284
|
4.3
|
4.9
|
1.0
|
OD2
|
B:ASP287
|
4.4
|
22.7
|
1.0
|
CB
|
B:ASP241
|
4.4
|
4.0
|
1.0
|
OG1
|
B:THR244
|
4.4
|
12.0
|
1.0
|
CA
|
B:ARG296
|
4.4
|
6.8
|
1.0
|
N
|
B:ASP287
|
4.5
|
21.9
|
1.0
|
N
|
B:ARG296
|
4.5
|
25.5
|
1.0
|
CA
|
B:ASP287
|
4.5
|
21.8
|
1.0
|
CB
|
B:VAL295
|
4.6
|
2.0
|
1.0
|
CA
|
B:VAL295
|
4.6
|
2.0
|
1.0
|
CB
|
B:ASP287
|
4.7
|
2.0
|
1.0
|
N
|
B:LEU292
|
4.8
|
73.4
|
1.0
|
CA
|
B:GLN291
|
4.9
|
5.6
|
1.0
|
CB
|
B:LEU292
|
4.9
|
2.8
|
1.0
|
N
|
B:VAL295
|
4.9
|
2.0
|
1.0
|
O
|
B:LEU292
|
4.9
|
7.6
|
1.0
|
C
|
B:LEU286
|
4.9
|
2.0
|
1.0
|
N
|
B:GLN291
|
5.0
|
19.0
|
1.0
|
|
Calcium binding site 2 out
of 4 in 1tah
Go back to
Calcium Binding Sites List in 1tah
Calcium binding site 2 out
of 4 in the The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate
 Mono view
 Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca320
b:43.5
occ:1.00
|
OD2
|
A:ASP241
|
2.4
|
32.8
|
1.0
|
OD1
|
A:ASP287
|
2.4
|
71.7
|
1.0
|
O
|
A:VAL295
|
2.5
|
14.5
|
1.0
|
O
|
A:GLN291
|
2.7
|
11.7
|
1.0
|
CG
|
A:ASP241
|
3.5
|
24.1
|
1.0
|
C
|
A:VAL295
|
3.6
|
2.0
|
1.0
|
CG
|
A:ASP287
|
3.6
|
10.0
|
1.0
|
C
|
A:GLN291
|
3.9
|
19.8
|
1.0
|
OG
|
A:SER243
|
4.1
|
23.4
|
1.0
|
OD1
|
A:ASP241
|
4.2
|
23.0
|
1.0
|
CA
|
A:ARG296
|
4.3
|
13.2
|
1.0
|
OD2
|
A:ASP287
|
4.3
|
29.6
|
1.0
|
OD1
|
A:ASN284
|
4.3
|
8.2
|
1.0
|
N
|
A:ARG296
|
4.4
|
25.2
|
1.0
|
OG1
|
A:THR244
|
4.4
|
3.2
|
1.0
|
CB
|
A:ASP241
|
4.4
|
6.2
|
1.0
|
CA
|
A:ASP287
|
4.5
|
28.4
|
1.0
|
N
|
A:ASP287
|
4.5
|
25.8
|
1.0
|
CB
|
A:VAL295
|
4.6
|
9.9
|
1.0
|
CA
|
A:VAL295
|
4.6
|
5.1
|
1.0
|
CB
|
A:ASP287
|
4.6
|
2.0
|
1.0
|
N
|
A:VAL295
|
4.9
|
2.0
|
1.0
|
N
|
A:LEU292
|
4.9
|
74.8
|
1.0
|
CA
|
A:GLN291
|
4.9
|
7.5
|
1.0
|
C
|
A:LEU286
|
5.0
|
2.0
|
1.0
|
O
|
A:LEU292
|
5.0
|
16.9
|
1.0
|
|
Calcium binding site 3 out
of 4 in 1tah
Go back to
Calcium Binding Sites List in 1tah
Calcium binding site 3 out
of 4 in the The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate
 Mono view
 Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Ca320
b:8.3
occ:1.00
|
OD2
|
C:ASP241
|
2.4
|
31.6
|
1.0
|
OD1
|
C:ASP287
|
2.4
|
75.5
|
1.0
|
O
|
C:VAL295
|
2.5
|
18.6
|
1.0
|
O
|
C:GLN291
|
2.9
|
2.0
|
1.0
|
CG
|
C:ASP241
|
3.5
|
12.6
|
1.0
|
C
|
C:VAL295
|
3.6
|
7.7
|
1.0
|
CG
|
C:ASP287
|
3.6
|
5.7
|
1.0
|
C
|
C:GLN291
|
4.1
|
18.2
|
1.0
|
CA
|
C:ARG296
|
4.2
|
6.9
|
1.0
|
OD2
|
C:ASP287
|
4.2
|
16.9
|
1.0
|
OG
|
C:SER243
|
4.2
|
22.1
|
1.0
|
OG1
|
C:THR244
|
4.2
|
16.6
|
1.0
|
OD1
|
C:ASP241
|
4.3
|
9.0
|
1.0
|
N
|
C:ARG296
|
4.3
|
24.7
|
1.0
|
OD1
|
C:ASN284
|
4.3
|
15.6
|
1.0
|
CB
|
C:ASP241
|
4.4
|
2.0
|
1.0
|
CA
|
C:ASP287
|
4.6
|
23.6
|
1.0
|
CB
|
C:VAL295
|
4.6
|
2.0
|
1.0
|
N
|
C:ASP287
|
4.6
|
20.6
|
1.0
|
CA
|
C:VAL295
|
4.6
|
2.0
|
1.0
|
CB
|
C:ASP287
|
4.6
|
2.0
|
1.0
|
N
|
C:VAL295
|
5.0
|
8.6
|
1.0
|
|
Calcium binding site 4 out
of 4 in 1tah
Go back to
Calcium Binding Sites List in 1tah
Calcium binding site 4 out
of 4 in the The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate
 Mono view
 Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 4 of The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Ca320
b:16.8
occ:1.00
|
OD1
|
D:ASP287
|
2.3
|
69.5
|
1.0
|
O
|
D:VAL295
|
2.5
|
18.8
|
1.0
|
OD2
|
D:ASP241
|
2.5
|
29.8
|
1.0
|
O
|
D:GLN291
|
2.9
|
2.0
|
1.0
|
CG
|
D:ASP287
|
3.5
|
2.0
|
1.0
|
C
|
D:VAL295
|
3.5
|
2.0
|
1.0
|
CG
|
D:ASP241
|
3.6
|
15.7
|
1.0
|
OD2
|
D:ASP287
|
4.1
|
22.7
|
1.0
|
CA
|
D:ARG296
|
4.1
|
2.0
|
1.0
|
C
|
D:GLN291
|
4.2
|
12.7
|
1.0
|
N
|
D:ARG296
|
4.2
|
22.5
|
1.0
|
OG1
|
D:THR244
|
4.3
|
15.0
|
1.0
|
OG
|
D:SER243
|
4.3
|
24.4
|
1.0
|
OD1
|
D:ASN284
|
4.3
|
2.0
|
1.0
|
OD1
|
D:ASP241
|
4.4
|
16.3
|
1.0
|
CB
|
D:ASP241
|
4.4
|
2.0
|
1.0
|
CA
|
D:ASP287
|
4.5
|
17.9
|
1.0
|
N
|
D:ASP287
|
4.5
|
16.2
|
1.0
|
CB
|
D:ASP287
|
4.5
|
2.0
|
1.0
|
CA
|
D:VAL295
|
4.6
|
8.2
|
1.0
|
CB
|
D:VAL295
|
4.6
|
2.0
|
1.0
|
N
|
D:VAL295
|
5.0
|
10.4
|
1.0
|
CG
|
D:ARG296
|
5.0
|
26.8
|
1.0
|
|
Reference:
M.E.Noble,
A.Cleasby,
L.N.Johnson,
M.R.Egmond,
L.G.Frenken.
The Crystal Structure of Triacylglycerol Lipase From Pseudomonas Glumae Reveals A Partially Redundant Catalytic Aspartate. Febs Lett. V. 331 123 1993.
ISSN: ISSN 0014-5793
PubMed: 8405390
DOI: 10.1016/0014-5793(93)80310-Q
Page generated: Thu Jul 11 22:58:45 2024
|