Magnesium in PDB 5g3t: The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
Enzymatic activity of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
All present enzymatic activity of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum:
1.4.3.23;
Protein crystallography data
The structure of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum, PDB code: 5g3t
was solved by
J.Krausze,
J.Rabe,
J.Moser,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
19.99 /
1.80
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
68.090,
89.160,
144.430,
90.00,
92.66,
90.00
|
|
R / Rfree (%)
|
15.7 /
19.2
|
Other elements in 5g3t:
The structure of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
(pdb code 5g3t). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the
The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum, PDB code: 5g3t:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
Magnesium binding site 1 out
of 6 in 5g3t
Go back to
Magnesium Binding Sites List in 5g3t
Magnesium binding site 1 out
of 6 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg420
b:21.0
occ:1.00
|
H
|
A:GLY16
|
2.2
|
15.9
|
1.0
|
|
H
|
A:GLY13
|
2.3
|
18.3
|
1.0
|
|
O1P
|
A:FDA419
|
2.7
|
15.0
|
1.0
|
|
O
|
A:ALA240
|
2.8
|
13.4
|
1.0
|
|
HB2
|
A:SER15
|
2.9
|
16.9
|
1.0
|
|
HA3
|
A:GLY13
|
3.0
|
17.1
|
1.0
|
|
N
|
A:GLY16
|
3.0
|
13.2
|
1.0
|
|
N
|
A:GLY13
|
3.0
|
15.3
|
1.0
|
|
HB2
|
A:ALA240
|
3.0
|
14.3
|
1.0
|
|
H52A
|
A:FDA419
|
3.2
|
15.2
|
1.0
|
|
CA
|
A:GLY13
|
3.3
|
14.3
|
1.0
|
|
HA3
|
A:GLY16
|
3.4
|
16.9
|
1.0
|
|
H
|
A:SER15
|
3.4
|
17.1
|
1.0
|
|
H4B
|
A:FDA419
|
3.4
|
19.4
|
1.0
|
|
HB1
|
A:ALA240
|
3.4
|
14.3
|
1.0
|
|
C
|
A:GLY13
|
3.5
|
13.4
|
1.0
|
|
HA3
|
A:GLY11
|
3.6
|
19.6
|
1.0
|
|
O5B
|
A:FDA419
|
3.6
|
16.9
|
1.0
|
|
CB
|
A:ALA240
|
3.6
|
11.9
|
1.0
|
|
C
|
A:GLY11
|
3.6
|
14.9
|
1.0
|
|
O
|
A:GLY11
|
3.6
|
19.3
|
1.0
|
|
O
|
A:GLY13
|
3.7
|
12.7
|
1.0
|
|
CA
|
A:GLY16
|
3.7
|
14.1
|
1.0
|
|
CB
|
A:SER15
|
3.8
|
14.0
|
1.0
|
|
C5B
|
A:FDA419
|
3.8
|
12.6
|
1.0
|
|
C
|
A:ALA240
|
3.8
|
12.0
|
1.0
|
|
N
|
A:SER15
|
3.8
|
14.2
|
1.0
|
|
P
|
A:FDA419
|
3.9
|
14.5
|
1.0
|
|
C
|
A:SER15
|
3.9
|
16.1
|
1.0
|
|
N
|
A:ALA12
|
4.0
|
17.4
|
1.0
|
|
CA
|
A:SER15
|
4.0
|
15.8
|
1.0
|
|
C
|
A:ALA12
|
4.1
|
15.6
|
1.0
|
|
C4B
|
A:FDA419
|
4.1
|
16.2
|
1.0
|
|
CA
|
A:GLY11
|
4.1
|
16.4
|
1.0
|
|
HA2
|
A:GLY13
|
4.2
|
17.1
|
1.0
|
|
O3P
|
A:FDA419
|
4.2
|
12.2
|
1.0
|
|
N
|
A:ILE14
|
4.3
|
14.4
|
1.0
|
|
HA2
|
A:GLY16
|
4.3
|
16.9
|
1.0
|
|
HB3
|
A:SER15
|
4.3
|
16.9
|
1.0
|
|
HA
|
A:ALA12
|
4.3
|
21.1
|
1.0
|
|
H
|
A:ALA12
|
4.3
|
20.9
|
1.0
|
|
CA
|
A:ALA240
|
4.3
|
14.9
|
1.0
|
|
H
|
A:LEU17
|
4.4
|
16.1
|
1.0
|
|
CA
|
A:ALA12
|
4.4
|
17.6
|
1.0
|
|
HB3
|
A:ALA240
|
4.4
|
14.3
|
1.0
|
|
HA2
|
A:GLY11
|
4.4
|
19.6
|
1.0
|
|
O
|
A:HOH2262
|
4.5
|
21.3
|
1.0
|
|
O2P
|
A:FDA419
|
4.5
|
16.8
|
1.0
|
|
H
|
A:ILE14
|
4.5
|
17.3
|
1.0
|
|
HA
|
A:ILE241
|
4.6
|
16.9
|
1.0
|
|
OG
|
A:SER15
|
4.7
|
18.4
|
1.0
|
|
PA
|
A:FDA419
|
4.7
|
12.6
|
1.0
|
|
C
|
A:ILE14
|
4.7
|
17.1
|
1.0
|
|
O4B
|
A:FDA419
|
4.7
|
18.4
|
1.0
|
|
HA
|
A:ALA240
|
4.8
|
17.9
|
1.0
|
|
H51A
|
A:FDA419
|
4.8
|
15.2
|
1.0
|
|
HG
|
A:SER15
|
4.8
|
22.1
|
1.0
|
|
N
|
A:ILE241
|
4.9
|
13.9
|
1.0
|
|
C
|
A:GLY16
|
4.9
|
15.3
|
1.0
|
|
N
|
A:LEU17
|
5.0
|
13.4
|
1.0
|
|
HA
|
A:SER15
|
5.0
|
18.9
|
1.0
|
|
Magnesium binding site 2 out
of 6 in 5g3t
Go back to
Magnesium Binding Sites List in 5g3t
Magnesium binding site 2 out
of 6 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg420
b:31.3
occ:1.00
|
O
|
B:HOH2129
|
2.6
|
35.1
|
1.0
|
|
O
|
B:VAL169
|
2.7
|
22.1
|
1.0
|
|
O
|
B:LYS103
|
2.8
|
19.1
|
1.0
|
|
O
|
B:HOH2136
|
2.9
|
29.8
|
1.0
|
|
HB2
|
B:ASN107
|
3.0
|
21.9
|
1.0
|
|
HG3
|
B:LYS103
|
3.1
|
24.3
|
1.0
|
|
HB2
|
B:MET106
|
3.2
|
22.3
|
1.0
|
|
HA
|
B:LYS103
|
3.2
|
19.8
|
1.0
|
|
H
|
B:ASN107
|
3.3
|
20.1
|
1.0
|
|
HA
|
B:THR170
|
3.3
|
21.0
|
1.0
|
|
HG2
|
B:LYS103
|
3.5
|
24.3
|
1.0
|
|
N
|
B:ASN107
|
3.6
|
16.8
|
1.0
|
|
HZ3
|
B:LYS103
|
3.6
|
36.0
|
1.0
|
|
CG
|
B:LYS103
|
3.7
|
20.2
|
1.0
|
|
C
|
B:LYS103
|
3.7
|
17.4
|
1.0
|
|
HB3
|
B:MET106
|
3.8
|
22.3
|
1.0
|
|
CA
|
B:LYS103
|
3.9
|
16.5
|
1.0
|
|
C
|
B:VAL169
|
3.9
|
23.7
|
1.0
|
|
CB
|
B:ASN107
|
3.9
|
18.3
|
1.0
|
|
CB
|
B:MET106
|
3.9
|
18.6
|
1.0
|
|
HA
|
B:ASN107
|
4.0
|
25.4
|
1.0
|
|
CA
|
B:ASN107
|
4.1
|
21.1
|
1.0
|
|
HG13
|
B:VAL169
|
4.1
|
26.5
|
1.0
|
|
HG23
|
B:THR170
|
4.1
|
31.4
|
1.0
|
|
C
|
B:MET106
|
4.2
|
19.5
|
1.0
|
|
CA
|
B:THR170
|
4.2
|
17.5
|
1.0
|
|
HB3
|
B:ASN107
|
4.3
|
21.9
|
1.0
|
|
CB
|
B:LYS103
|
4.3
|
17.5
|
1.0
|
|
O
|
B:HOH2186
|
4.4
|
44.5
|
1.0
|
|
N
|
B:THR170
|
4.5
|
20.0
|
1.0
|
|
CA
|
B:MET106
|
4.5
|
19.1
|
1.0
|
|
NZ
|
B:LYS103
|
4.5
|
30.0
|
1.0
|
|
H
|
B:MET106
|
4.6
|
22.0
|
1.0
|
|
HG11
|
B:VAL169
|
4.6
|
26.5
|
1.0
|
|
O
|
B:HOH2138
|
4.6
|
36.6
|
1.0
|
|
OD2
|
B:ASP171
|
4.7
|
45.6
|
1.0
|
|
CG1
|
B:VAL169
|
4.8
|
22.1
|
1.0
|
|
HB2
|
B:LYS103
|
4.8
|
21.1
|
1.0
|
|
O
|
B:HOH2035
|
4.8
|
30.0
|
1.0
|
|
N
|
B:MET106
|
4.9
|
18.3
|
1.0
|
|
CG2
|
B:THR170
|
4.9
|
26.1
|
1.0
|
|
HA
|
B:VAL169
|
4.9
|
20.2
|
1.0
|
|
O
|
B:LEU102
|
4.9
|
16.7
|
1.0
|
|
HZ1
|
B:LYS103
|
4.9
|
36.0
|
1.0
|
|
HZ2
|
B:LYS103
|
4.9
|
36.0
|
1.0
|
|
O
|
B:MET106
|
4.9
|
22.2
|
1.0
|
|
CG
|
B:ASN107
|
4.9
|
27.0
|
1.0
|
|
N
|
B:ARG104
|
4.9
|
16.4
|
1.0
|
|
HE3
|
B:LYS103
|
5.0
|
32.2
|
1.0
|
|
HG21
|
B:THR170
|
5.0
|
31.4
|
1.0
|
|
CD
|
B:LYS103
|
5.0
|
15.2
|
1.0
|
|
CA
|
B:VAL169
|
5.0
|
16.8
|
1.0
|
|
Magnesium binding site 3 out
of 6 in 5g3t
Go back to
Magnesium Binding Sites List in 5g3t
Magnesium binding site 3 out
of 6 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg421
b:23.6
occ:1.00
|
H
|
B:GLY16
|
2.2
|
20.2
|
1.0
|
|
H
|
B:GLY13
|
2.4
|
22.4
|
1.0
|
|
O
|
B:ALA240
|
2.7
|
19.2
|
1.0
|
|
O1P
|
B:FDA419
|
2.8
|
15.9
|
1.0
|
|
HB2
|
B:SER15
|
2.9
|
22.6
|
1.0
|
|
HB2
|
B:ALA240
|
3.0
|
18.5
|
1.0
|
|
N
|
B:GLY16
|
3.0
|
16.8
|
1.0
|
|
N
|
B:GLY13
|
3.1
|
18.7
|
1.0
|
|
HA3
|
B:GLY13
|
3.2
|
20.9
|
1.0
|
|
H52A
|
B:FDA419
|
3.2
|
21.6
|
1.0
|
|
H4B
|
B:FDA419
|
3.3
|
20.6
|
1.0
|
|
HA3
|
B:GLY16
|
3.4
|
22.6
|
1.0
|
|
HB1
|
B:ALA240
|
3.4
|
18.5
|
1.0
|
|
CA
|
B:GLY13
|
3.5
|
17.4
|
1.0
|
|
HA3
|
B:GLY11
|
3.5
|
24.7
|
1.0
|
|
H
|
B:SER15
|
3.5
|
21.8
|
1.0
|
|
O5B
|
B:FDA419
|
3.6
|
17.8
|
1.0
|
|
CB
|
B:ALA240
|
3.6
|
15.4
|
1.0
|
|
C
|
B:GLY11
|
3.7
|
18.8
|
1.0
|
|
C
|
B:ALA240
|
3.7
|
16.6
|
1.0
|
|
C
|
B:GLY13
|
3.7
|
15.8
|
1.0
|
|
O
|
B:GLY11
|
3.7
|
20.7
|
1.0
|
|
CA
|
B:GLY16
|
3.7
|
18.8
|
1.0
|
|
C5B
|
B:FDA419
|
3.7
|
18.0
|
1.0
|
|
CB
|
B:SER15
|
3.8
|
18.8
|
1.0
|
|
O
|
B:GLY13
|
3.9
|
15.3
|
1.0
|
|
P
|
B:FDA419
|
3.9
|
17.5
|
1.0
|
|
N
|
B:SER15
|
3.9
|
18.1
|
1.0
|
|
N
|
B:ALA12
|
4.0
|
18.6
|
1.0
|
|
C4B
|
B:FDA419
|
4.0
|
17.2
|
1.0
|
|
C
|
B:SER15
|
4.0
|
19.8
|
1.0
|
|
CA
|
B:GLY11
|
4.0
|
20.6
|
1.0
|
|
CA
|
B:SER15
|
4.1
|
19.2
|
1.0
|
|
C
|
B:ALA12
|
4.2
|
17.3
|
1.0
|
|
HA2
|
B:GLY16
|
4.2
|
22.6
|
1.0
|
|
O3P
|
B:FDA419
|
4.2
|
18.1
|
1.0
|
|
CA
|
B:ALA240
|
4.3
|
17.7
|
1.0
|
|
HB3
|
B:SER15
|
4.3
|
22.6
|
1.0
|
|
H
|
B:ALA12
|
4.3
|
22.3
|
1.0
|
|
HA2
|
B:GLY11
|
4.3
|
24.7
|
1.0
|
|
HA
|
B:ALA12
|
4.3
|
20.4
|
1.0
|
|
O
|
B:HOH2226
|
4.4
|
24.5
|
1.0
|
|
HB3
|
B:ALA240
|
4.4
|
18.5
|
1.0
|
|
HA2
|
B:GLY13
|
4.4
|
20.9
|
1.0
|
|
CA
|
B:ALA12
|
4.4
|
17.0
|
1.0
|
|
N
|
B:ILE14
|
4.4
|
17.9
|
1.0
|
|
O2P
|
B:FDA419
|
4.5
|
18.4
|
1.0
|
|
H
|
B:LEU17
|
4.5
|
20.8
|
1.0
|
|
HA
|
B:ILE241
|
4.6
|
21.8
|
1.0
|
|
PA
|
B:FDA419
|
4.6
|
14.4
|
1.0
|
|
O4B
|
B:FDA419
|
4.6
|
16.8
|
1.0
|
|
H
|
B:ILE14
|
4.7
|
21.4
|
1.0
|
|
HA
|
B:ALA240
|
4.7
|
21.2
|
1.0
|
|
OG
|
B:SER15
|
4.7
|
21.0
|
1.0
|
|
H51A
|
B:FDA419
|
4.8
|
21.6
|
1.0
|
|
N
|
B:ILE241
|
4.8
|
18.7
|
1.0
|
|
C
|
B:ILE14
|
4.9
|
16.4
|
1.0
|
|
HG
|
B:SER15
|
4.9
|
25.2
|
1.0
|
|
C
|
B:GLY16
|
5.0
|
19.7
|
1.0
|
|
Magnesium binding site 4 out
of 6 in 5g3t
Go back to
Magnesium Binding Sites List in 5g3t
Magnesium binding site 4 out
of 6 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg420
b:36.2
occ:1.00
|
O
|
D:HOH2345
|
2.3
|
45.1
|
1.0
|
|
O
|
D:ALA360
|
2.8
|
14.6
|
1.0
|
|
O
|
D:HOH2280
|
3.0
|
29.1
|
1.0
|
|
HB2
|
D:ALA360
|
3.1
|
17.9
|
1.0
|
|
HB3
|
D:PRO266
|
3.2
|
15.7
|
1.0
|
|
HA
|
D:ALA360
|
3.4
|
14.8
|
1.0
|
|
OH
|
D:TYR358
|
3.4
|
16.3
|
1.0
|
|
O
|
D:HOH2245
|
3.4
|
22.6
|
1.0
|
|
HH
|
D:TYR358
|
3.6
|
19.6
|
1.0
|
|
HD3
|
D:PRO266
|
3.6
|
19.1
|
1.0
|
|
C
|
D:ALA360
|
3.6
|
17.6
|
1.0
|
|
O
|
C:HOH2250
|
3.7
|
31.2
|
1.0
|
|
CA
|
D:ALA360
|
3.8
|
12.3
|
1.0
|
|
CB
|
D:ALA360
|
3.9
|
15.0
|
1.0
|
|
HG3
|
D:PRO266
|
4.0
|
19.2
|
1.0
|
|
CB
|
D:PRO266
|
4.1
|
13.1
|
1.0
|
|
CD
|
D:PRO266
|
4.3
|
15.9
|
1.0
|
|
HB3
|
D:ALA360
|
4.3
|
17.9
|
1.0
|
|
CG
|
D:PRO266
|
4.3
|
16.0
|
1.0
|
|
HD22
|
D:ASN316
|
4.5
|
28.3
|
1.0
|
|
CZ
|
D:TYR358
|
4.5
|
13.7
|
1.0
|
|
HB1
|
D:ALA360
|
4.6
|
17.9
|
1.0
|
|
HE2
|
D:TYR358
|
4.7
|
18.5
|
1.0
|
|
O
|
D:HOH2142
|
4.7
|
31.2
|
1.0
|
|
HB2
|
D:PRO266
|
4.7
|
15.7
|
1.0
|
|
HA
|
D:PRO266
|
4.7
|
13.3
|
1.0
|
|
N
|
D:PRO266
|
4.8
|
14.2
|
1.0
|
|
O
|
C:HOH2247
|
4.8
|
36.9
|
1.0
|
|
CA
|
D:PRO266
|
4.8
|
11.1
|
1.0
|
|
N
|
D:HIS361
|
4.9
|
14.9
|
1.0
|
|
OD1
|
D:ASN316
|
4.9
|
19.7
|
1.0
|
|
Magnesium binding site 5 out
of 6 in 5g3t
Go back to
Magnesium Binding Sites List in 5g3t
Magnesium binding site 5 out
of 6 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg421
b:21.8
occ:1.00
|
H
|
D:GLY16
|
2.2
|
15.7
|
1.0
|
|
H
|
D:GLY13
|
2.3
|
17.4
|
1.0
|
|
O
|
D:ALA240
|
2.8
|
15.4
|
1.0
|
|
O1P
|
D:FDA419
|
2.8
|
13.0
|
1.0
|
|
N
|
D:GLY13
|
2.9
|
14.5
|
1.0
|
|
HB2
|
D:SER15
|
3.0
|
22.4
|
1.0
|
|
HA3
|
D:GLY13
|
3.0
|
17.2
|
1.0
|
|
N
|
D:GLY16
|
3.0
|
13.1
|
1.0
|
|
HB2
|
D:ALA240
|
3.0
|
19.6
|
1.0
|
|
H51A
|
D:FDA419
|
3.1
|
17.6
|
1.0
|
|
CA
|
D:GLY13
|
3.3
|
14.3
|
1.0
|
|
HA3
|
D:GLY16
|
3.3
|
16.5
|
1.0
|
|
H4B
|
D:FDA419
|
3.4
|
14.5
|
1.0
|
|
HB1
|
D:ALA240
|
3.4
|
19.6
|
1.0
|
|
H
|
D:SER15
|
3.5
|
14.6
|
1.0
|
|
HA3
|
D:GLY11
|
3.5
|
16.7
|
1.0
|
|
C
|
D:GLY13
|
3.6
|
14.1
|
1.0
|
|
C
|
D:GLY11
|
3.6
|
16.0
|
1.0
|
|
O
|
D:GLY11
|
3.6
|
17.4
|
1.0
|
|
CB
|
D:ALA240
|
3.6
|
16.3
|
1.0
|
|
CA
|
D:GLY16
|
3.7
|
13.8
|
1.0
|
|
O5B
|
D:FDA419
|
3.7
|
13.9
|
1.0
|
|
O
|
D:GLY13
|
3.7
|
15.3
|
1.0
|
|
C5B
|
D:FDA419
|
3.7
|
14.7
|
1.0
|
|
C
|
D:ALA240
|
3.8
|
13.8
|
1.0
|
|
CB
|
D:SER15
|
3.8
|
18.7
|
1.0
|
|
N
|
D:SER15
|
3.9
|
12.2
|
1.0
|
|
N
|
D:ALA12
|
3.9
|
14.1
|
1.0
|
|
P
|
D:FDA419
|
3.9
|
14.2
|
1.0
|
|
C
|
D:SER15
|
4.0
|
16.1
|
1.0
|
|
C
|
D:ALA12
|
4.0
|
17.7
|
1.0
|
|
CA
|
D:GLY11
|
4.0
|
13.9
|
1.0
|
|
C4B
|
D:FDA419
|
4.1
|
12.1
|
1.0
|
|
CA
|
D:SER15
|
4.1
|
16.0
|
1.0
|
|
HA
|
D:ALA12
|
4.2
|
18.2
|
1.0
|
|
HA2
|
D:GLY16
|
4.2
|
16.5
|
1.0
|
|
HA2
|
D:GLY13
|
4.2
|
17.2
|
1.0
|
|
HB3
|
D:SER15
|
4.2
|
22.4
|
1.0
|
|
O3P
|
D:FDA419
|
4.3
|
14.3
|
1.0
|
|
H
|
D:ALA12
|
4.3
|
17.0
|
1.0
|
|
CA
|
D:ALA12
|
4.3
|
15.2
|
1.0
|
|
CA
|
D:ALA240
|
4.3
|
14.4
|
1.0
|
|
N
|
D:ILE14
|
4.3
|
15.4
|
1.0
|
|
HA2
|
D:GLY11
|
4.4
|
16.7
|
1.0
|
|
HB3
|
D:ALA240
|
4.4
|
19.6
|
1.0
|
|
H
|
D:LEU17
|
4.5
|
16.6
|
1.0
|
|
O2P
|
D:FDA419
|
4.5
|
15.2
|
1.0
|
|
O
|
D:HOH2224
|
4.6
|
18.0
|
1.0
|
|
H
|
D:ILE14
|
4.6
|
18.5
|
1.0
|
|
HA
|
D:ILE241
|
4.7
|
14.2
|
1.0
|
|
O4B
|
D:FDA419
|
4.7
|
14.1
|
1.0
|
|
PA
|
D:FDA419
|
4.7
|
12.9
|
1.0
|
|
H52A
|
D:FDA419
|
4.7
|
17.6
|
1.0
|
|
C
|
D:ILE14
|
4.8
|
16.1
|
1.0
|
|
HA
|
D:ALA240
|
4.8
|
17.2
|
1.0
|
|
OG
|
D:SER15
|
4.8
|
24.4
|
1.0
|
|
N
|
D:ILE241
|
4.9
|
13.2
|
1.0
|
|
C
|
D:GLY16
|
4.9
|
14.9
|
1.0
|
|
HG
|
D:SER15
|
5.0
|
29.3
|
1.0
|
|
N
|
D:LEU17
|
5.0
|
13.8
|
1.0
|
|
Magnesium binding site 6 out
of 6 in 5g3t
Go back to
Magnesium Binding Sites List in 5g3t
Magnesium binding site 6 out
of 6 in the The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of The Structure of the L-Tryptophan Oxidase Vioa From Chromobacterium Violaceum within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg422
b:21.2
occ:1.00
|
HO4'
|
D:FDA419
|
2.0
|
19.8
|
1.0
|
|
H
|
D:ILE14
|
2.2
|
18.5
|
1.0
|
|
O1A
|
D:FDA419
|
2.6
|
12.5
|
1.0
|
|
O
|
D:GLY44
|
2.7
|
16.1
|
1.0
|
|
HG23
|
D:ILE14
|
2.9
|
18.5
|
1.0
|
|
O4'
|
D:FDA419
|
2.9
|
16.5
|
1.0
|
|
N
|
D:ILE14
|
3.0
|
15.4
|
1.0
|
|
HG13
|
D:ILE47
|
3.1
|
20.6
|
1.0
|
|
O5'
|
D:FDA419
|
3.1
|
11.1
|
1.0
|
|
HA3
|
D:GLY13
|
3.1
|
17.2
|
1.0
|
|
HD13
|
D:ILE47
|
3.1
|
19.1
|
1.0
|
|
H
|
D:ARG46
|
3.2
|
18.0
|
1.0
|
|
HA2
|
D:GLY13
|
3.3
|
17.2
|
1.0
|
|
H
|
D:ILE47
|
3.3
|
16.9
|
1.0
|
|
HB
|
D:ILE14
|
3.4
|
17.6
|
1.0
|
|
CA
|
D:GLY13
|
3.6
|
14.3
|
1.0
|
|
HA3
|
D:GLY45
|
3.6
|
19.3
|
1.0
|
|
O1P
|
D:FDA419
|
3.6
|
13.0
|
1.0
|
|
CG2
|
D:ILE14
|
3.7
|
15.4
|
1.0
|
|
C
|
D:GLY44
|
3.7
|
17.2
|
1.0
|
|
CD1
|
D:ILE47
|
3.7
|
15.9
|
1.0
|
|
CG1
|
D:ILE47
|
3.8
|
17.1
|
1.0
|
|
C
|
D:GLY13
|
3.8
|
14.1
|
1.0
|
|
C4'
|
D:FDA419
|
3.8
|
14.8
|
1.0
|
|
N
|
D:ARG46
|
3.8
|
15.0
|
1.0
|
|
HB
|
D:ILE47
|
3.8
|
17.2
|
1.0
|
|
HD12
|
D:ILE47
|
3.9
|
19.1
|
1.0
|
|
CB
|
D:ILE14
|
3.9
|
14.7
|
1.0
|
|
C5'
|
D:FDA419
|
3.9
|
11.9
|
1.0
|
|
P
|
D:FDA419
|
3.9
|
14.2
|
1.0
|
|
PA
|
D:FDA419
|
3.9
|
12.9
|
1.0
|
|
HD12
|
D:ILE188
|
3.9
|
22.1
|
1.0
|
|
N
|
D:ILE47
|
3.9
|
14.1
|
1.0
|
|
CA
|
D:ILE14
|
4.0
|
14.5
|
1.0
|
|
H5'2
|
D:FDA419
|
4.0
|
14.3
|
1.0
|
|
HG22
|
D:ILE14
|
4.0
|
18.5
|
1.0
|
|
H4'
|
D:FDA419
|
4.1
|
17.8
|
1.0
|
|
HB2
|
D:ARG46
|
4.2
|
16.3
|
1.0
|
|
CA
|
D:GLY45
|
4.3
|
16.1
|
1.0
|
|
CB
|
D:ILE47
|
4.3
|
14.3
|
1.0
|
|
O3P
|
D:FDA419
|
4.3
|
14.3
|
1.0
|
|
HO2'
|
D:FDA419
|
4.3
|
18.1
|
1.0
|
|
HA2
|
D:GLY44
|
4.3
|
20.5
|
1.0
|
|
H
|
D:SER15
|
4.4
|
14.6
|
1.0
|
|
N
|
D:GLY45
|
4.4
|
17.1
|
1.0
|
|
HG21
|
D:ILE14
|
4.4
|
18.5
|
1.0
|
|
C
|
D:GLY45
|
4.4
|
15.5
|
1.0
|
|
O5B
|
D:FDA419
|
4.4
|
13.9
|
1.0
|
|
C
|
D:ARG46
|
4.6
|
14.6
|
1.0
|
|
HG12
|
D:ILE47
|
4.6
|
20.6
|
1.0
|
|
HA
|
D:ILE14
|
4.6
|
17.4
|
1.0
|
|
CA
|
D:ARG46
|
4.6
|
14.1
|
1.0
|
|
HD11
|
D:ILE47
|
4.6
|
19.1
|
1.0
|
|
CA
|
D:GLY44
|
4.7
|
17.1
|
1.0
|
|
HD13
|
D:ILE188
|
4.7
|
22.1
|
1.0
|
|
CA
|
D:ILE47
|
4.7
|
13.6
|
1.0
|
|
CD1
|
D:ILE188
|
4.8
|
18.4
|
1.0
|
|
H5'1
|
D:FDA419
|
4.9
|
14.3
|
1.0
|
|
CB
|
D:ARG46
|
4.9
|
13.6
|
1.0
|
|
N
|
D:GLY13
|
5.0
|
14.5
|
1.0
|
|
N
|
D:SER15
|
5.0
|
12.2
|
1.0
|
|
O
|
D:GLY13
|
5.0
|
15.3
|
1.0
|
|
Reference:
J.Fuller,
R.Roepke,
J.Krausze,
K.E.Rennhack,
N.P.Daniel,
W.Blankenfeldt,
S.Schulz,
D.Jahn,
J.Moser.
Biosynthesis of Violacein: Structure and Function of L-Tryptophan Oxidase Vioa Chromobacterium Violaceum J.Biol.Chem. V. 291 20068 2016.
ISSN: ISSN 0021-9258
PubMed: 27466367
DOI: 10.1074/JBC.M116.741561
Page generated: Sun Sep 29 04:35:47 2024
|
