Sodium in PDB 7rof: Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound
Enzymatic activity of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound
All present enzymatic activity of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound:
4.2.1.20;
Protein crystallography data
The structure of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound, PDB code: 7rof
was solved by
P.M.Higgins,
A.R.Buller,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.70 /
2.39
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
57.402,
82.658,
322.255,
90,
90,
90
|
R / Rfree (%)
|
22.7 /
27.1
|
Sodium Binding Sites:
The binding sites of Sodium atom in the Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound
(pdb code 7rof). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 4 binding sites of Sodium where determined in the
Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound, PDB code: 7rof:
Jump to Sodium binding site number:
1;
2;
3;
4;
Sodium binding site 1 out
of 4 in 7rof
Go back to
Sodium Binding Sites List in 7rof
Sodium binding site 1 out
of 4 in the Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na402
b:51.2
occ:1.00
|
O
|
A:GLY303
|
2.6
|
52.2
|
1.0
|
O
|
A:SER263
|
2.8
|
51.0
|
1.0
|
O
|
A:TYR301
|
2.9
|
56.3
|
1.0
|
O
|
A:GLY227
|
3.0
|
50.3
|
1.0
|
OG
|
A:SER265
|
3.4
|
59.4
|
1.0
|
OE2
|
A:GLU251
|
3.7
|
60.1
|
1.0
|
C
|
A:GLY303
|
3.8
|
53.0
|
1.0
|
C
|
A:SER263
|
4.0
|
51.2
|
1.0
|
C
|
A:TYR301
|
4.0
|
58.0
|
1.0
|
C
|
A:GLY227
|
4.0
|
50.4
|
1.0
|
CB
|
A:SER263
|
4.1
|
50.7
|
1.0
|
CB
|
A:SER265
|
4.3
|
58.5
|
1.0
|
O
|
A:LEU299
|
4.3
|
52.6
|
1.0
|
CA
|
A:GLY227
|
4.4
|
50.1
|
1.0
|
O
|
A:VAL226
|
4.4
|
53.3
|
1.0
|
N
|
A:GLY303
|
4.5
|
56.4
|
1.0
|
N
|
A:SER265
|
4.5
|
55.5
|
1.0
|
CB
|
A:VAL304
|
4.5
|
48.9
|
1.0
|
CB
|
A:TYR301
|
4.6
|
62.3
|
1.0
|
CA
|
A:SER263
|
4.6
|
51.5
|
1.0
|
CD2
|
A:TYR301
|
4.6
|
68.2
|
1.0
|
CD
|
A:GLU251
|
4.6
|
59.6
|
1.0
|
C
|
A:PRO302
|
4.6
|
58.1
|
1.0
|
N
|
A:VAL304
|
4.7
|
52.2
|
1.0
|
CA
|
A:TYR301
|
4.7
|
60.0
|
1.0
|
CA
|
A:GLY303
|
4.8
|
55.8
|
1.0
|
CA
|
A:VAL304
|
4.8
|
50.2
|
1.0
|
CG
|
A:GLU251
|
4.9
|
56.2
|
1.0
|
N
|
A:TYR301
|
4.9
|
57.9
|
1.0
|
O
|
A:PRO302
|
5.0
|
58.5
|
1.0
|
N
|
A:PRO302
|
5.0
|
59.0
|
1.0
|
|
Sodium binding site 2 out
of 4 in 7rof
Go back to
Sodium Binding Sites List in 7rof
Sodium binding site 2 out
of 4 in the Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na401
b:85.6
occ:1.00
|
O
|
B:SER263
|
2.6
|
103.5
|
1.0
|
O
|
B:TYR301
|
2.7
|
88.0
|
1.0
|
O
|
B:GLY303
|
2.9
|
102.0
|
1.0
|
OG
|
B:SER265
|
3.2
|
102.7
|
1.0
|
O
|
B:GLY227
|
3.2
|
79.9
|
1.0
|
C
|
B:SER263
|
3.8
|
105.1
|
1.0
|
C
|
B:TYR301
|
3.9
|
88.3
|
1.0
|
C
|
B:GLY303
|
4.0
|
101.2
|
1.0
|
CB
|
B:SER263
|
4.1
|
107.3
|
1.0
|
CB
|
B:SER265
|
4.2
|
101.7
|
1.0
|
O
|
B:LEU299
|
4.2
|
86.8
|
1.0
|
C
|
B:GLY227
|
4.2
|
77.2
|
1.0
|
N
|
B:SER265
|
4.3
|
103.4
|
1.0
|
CA
|
B:SER263
|
4.4
|
106.4
|
1.0
|
C
|
B:PRO302
|
4.5
|
107.9
|
1.0
|
O
|
B:PRO302
|
4.5
|
108.5
|
1.0
|
CB
|
B:TYR301
|
4.6
|
91.0
|
1.0
|
CA
|
B:TYR301
|
4.6
|
89.9
|
1.0
|
N
|
B:GLY303
|
4.6
|
105.1
|
1.0
|
CA
|
B:GLY227
|
4.6
|
76.8
|
1.0
|
O
|
B:VAL226
|
4.7
|
79.3
|
1.0
|
N
|
B:TYR301
|
4.7
|
89.9
|
1.0
|
CB
|
B:VAL304
|
4.7
|
97.9
|
1.0
|
N
|
B:VAL304
|
4.7
|
99.2
|
1.0
|
OE2
|
B:GLU251
|
4.8
|
96.8
|
1.0
|
N
|
B:ALA264
|
4.8
|
105.9
|
1.0
|
CA
|
B:VAL304
|
4.8
|
97.0
|
1.0
|
N
|
B:PRO302
|
4.9
|
110.5
|
1.0
|
CA
|
B:SER265
|
4.9
|
102.6
|
1.0
|
CA
|
B:GLY303
|
4.9
|
103.0
|
1.0
|
CA
|
B:PRO302
|
5.0
|
110.6
|
1.0
|
CD2
|
B:TYR301
|
5.0
|
94.8
|
1.0
|
|
Sodium binding site 3 out
of 4 in 7rof
Go back to
Sodium Binding Sites List in 7rof
Sodium binding site 3 out
of 4 in the Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 3 of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Na401
b:85.2
occ:1.00
|
O
|
C:GLY303
|
2.7
|
81.1
|
1.0
|
O
|
C:SER263
|
2.7
|
99.4
|
1.0
|
O
|
C:TYR301
|
2.8
|
104.9
|
1.0
|
O
|
C:GLY227
|
2.9
|
80.8
|
1.0
|
OG
|
C:SER265
|
3.2
|
101.5
|
1.0
|
OE2
|
C:GLU251
|
3.8
|
82.7
|
1.0
|
C
|
C:GLY303
|
3.9
|
82.3
|
1.0
|
C
|
C:GLY227
|
3.9
|
79.3
|
1.0
|
C
|
C:SER263
|
3.9
|
101.1
|
1.0
|
C
|
C:TYR301
|
4.0
|
106.2
|
1.0
|
CA
|
C:GLY227
|
4.2
|
78.2
|
1.0
|
CB
|
C:SER263
|
4.2
|
101.5
|
1.0
|
CB
|
C:SER265
|
4.2
|
101.8
|
1.0
|
O
|
C:LEU299
|
4.3
|
97.6
|
1.0
|
N
|
C:SER265
|
4.4
|
102.1
|
1.0
|
CB
|
C:VAL304
|
4.6
|
77.6
|
1.0
|
CA
|
C:SER263
|
4.6
|
102.4
|
1.0
|
O
|
C:VAL226
|
4.6
|
78.1
|
1.0
|
N
|
C:VAL304
|
4.7
|
80.9
|
1.0
|
CD
|
C:GLU251
|
4.7
|
81.6
|
1.0
|
CA
|
C:VAL304
|
4.7
|
78.1
|
1.0
|
C
|
C:PRO302
|
4.7
|
87.2
|
1.0
|
CB
|
C:TYR301
|
4.7
|
105.6
|
1.0
|
CD2
|
C:TYR301
|
4.7
|
106.0
|
1.0
|
N
|
C:GLY303
|
4.7
|
86.2
|
1.0
|
CA
|
C:TYR301
|
4.8
|
106.1
|
1.0
|
O
|
C:PRO302
|
4.8
|
87.6
|
1.0
|
N
|
C:TYR301
|
4.9
|
105.1
|
1.0
|
CG2
|
C:VAL304
|
4.9
|
75.6
|
1.0
|
CA
|
C:GLY303
|
4.9
|
85.2
|
1.0
|
N
|
C:ALA264
|
5.0
|
102.0
|
1.0
|
CA
|
C:SER265
|
5.0
|
102.7
|
1.0
|
CG
|
C:GLU251
|
5.0
|
78.8
|
1.0
|
|
Sodium binding site 4 out
of 4 in 7rof
Go back to
Sodium Binding Sites List in 7rof
Sodium binding site 4 out
of 4 in the Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 4 of Engineered Tryptophan Synthase B-Subunit From Pyrococcus Furiosus, PFTRPB2B9-H275E with L-Trp Non-Covalently Bound within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Na402
b:87.6
occ:1.00
|
O
|
D:GLY303
|
2.6
|
79.7
|
1.0
|
O
|
D:SER263
|
2.7
|
107.3
|
1.0
|
O
|
D:TYR301
|
2.8
|
87.9
|
1.0
|
OG
|
D:SER265
|
3.1
|
102.0
|
1.0
|
O
|
D:GLY227
|
3.1
|
78.2
|
1.0
|
C
|
D:GLY303
|
3.8
|
79.6
|
1.0
|
C
|
D:SER263
|
3.9
|
108.8
|
1.0
|
C
|
D:TYR301
|
3.9
|
91.0
|
1.0
|
CB
|
D:SER263
|
4.0
|
108.9
|
1.0
|
CB
|
D:SER265
|
4.1
|
102.1
|
1.0
|
C
|
D:GLY227
|
4.1
|
75.1
|
1.0
|
O
|
D:PRO302
|
4.2
|
89.5
|
1.0
|
C
|
D:PRO302
|
4.3
|
89.9
|
1.0
|
N
|
D:SER265
|
4.3
|
106.9
|
1.0
|
O
|
D:LEU299
|
4.4
|
84.6
|
1.0
|
N
|
D:GLY303
|
4.4
|
87.3
|
1.0
|
CA
|
D:SER263
|
4.5
|
109.0
|
1.0
|
CA
|
D:GLY227
|
4.5
|
74.6
|
1.0
|
N
|
D:VAL304
|
4.6
|
76.4
|
1.0
|
OE2
|
D:GLU251
|
4.6
|
87.8
|
1.0
|
O
|
D:VAL226
|
4.6
|
75.8
|
1.0
|
CB
|
D:VAL304
|
4.7
|
71.7
|
1.0
|
CA
|
D:GLY303
|
4.7
|
83.6
|
1.0
|
CA
|
D:TYR301
|
4.7
|
91.8
|
1.0
|
CA
|
D:VAL304
|
4.7
|
72.6
|
1.0
|
CB
|
D:TYR301
|
4.8
|
89.3
|
1.0
|
N
|
D:TYR301
|
4.8
|
91.6
|
1.0
|
CA
|
D:SER265
|
4.8
|
104.5
|
1.0
|
N
|
D:PRO302
|
4.9
|
93.1
|
1.0
|
CA
|
D:PRO302
|
4.9
|
93.3
|
1.0
|
CD2
|
D:TYR301
|
5.0
|
86.0
|
1.0
|
N
|
D:ALA264
|
5.0
|
110.8
|
1.0
|
|
Reference:
P.M.Higgins,
A.R.Buller.
Direct Assessment of Promiscuity During Protein Engineering By Substrate Multiplexed Screening To Be Published.
Page generated: Wed Oct 9 08:39:21 2024
|