Potassium in PDB 1ax4: Tryptophanase From Proteus Vulgaris
Enzymatic activity of Tryptophanase From Proteus Vulgaris
All present enzymatic activity of Tryptophanase From Proteus Vulgaris:
4.1.99.1;
Protein crystallography data
The structure of Tryptophanase From Proteus Vulgaris, PDB code: 1ax4
was solved by
M.N.Isupov,
A.A.Antson,
E.J.Dodson,
G.G.Dodson,
I.S.Dementieva,
L.N.Zakomirdina,
K.S.Wilson,
Z.Dauter,
A.A.Lebedev,
E.H.Harutyunyan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
18.00 /
2.10
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
114.990,
118.230,
153.680,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.7 /
22.7
|
Potassium Binding Sites:
The binding sites of Potassium atom in the Tryptophanase From Proteus Vulgaris
(pdb code 1ax4). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the
Tryptophanase From Proteus Vulgaris, PDB code: 1ax4:
Jump to Potassium binding site number:
1;
2;
3;
4;
Potassium binding site 1 out
of 4 in 1ax4
Go back to
Potassium Binding Sites List in 1ax4
Potassium binding site 1 out
of 4 in the Tryptophanase From Proteus Vulgaris
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Tryptophanase From Proteus Vulgaris within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K500
b:12.2
occ:1.00
|
OE1
|
B:GLU70
|
2.6
|
9.1
|
1.0
|
O
|
A:GLY53
|
2.8
|
7.7
|
1.0
|
O
|
B:HOH515
|
2.9
|
11.2
|
1.0
|
O
|
A:HOH544
|
2.9
|
15.9
|
1.0
|
O
|
A:ASN271
|
2.9
|
10.5
|
1.0
|
O
|
A:HOH542
|
3.1
|
15.3
|
1.0
|
O
|
B:GLU70
|
3.4
|
11.7
|
1.0
|
C
|
A:GLY53
|
3.6
|
12.9
|
1.0
|
CD
|
B:GLU70
|
3.8
|
20.1
|
1.0
|
CB
|
B:GLU70
|
3.9
|
7.6
|
1.0
|
C
|
A:ASN271
|
3.9
|
6.8
|
1.0
|
CA
|
A:GLY53
|
3.9
|
10.2
|
1.0
|
CB
|
A:ASN271
|
3.9
|
3.9
|
1.0
|
CA
|
A:ASN271
|
4.1
|
5.3
|
1.0
|
CA
|
B:GLU70
|
4.1
|
5.2
|
1.0
|
C
|
B:GLU70
|
4.2
|
8.4
|
1.0
|
CA
|
B:ALA305
|
4.3
|
10.8
|
1.0
|
N
|
B:GLY306
|
4.3
|
7.2
|
1.0
|
CG
|
B:GLU70
|
4.3
|
9.8
|
1.0
|
O
|
B:HOH508
|
4.4
|
9.1
|
1.0
|
N
|
A:THR54
|
4.7
|
7.9
|
1.0
|
OE2
|
B:GLU70
|
4.8
|
10.9
|
1.0
|
CE
|
A:LYS265
|
4.8
|
9.6
|
1.0
|
CB
|
B:ALA305
|
4.8
|
8.1
|
1.0
|
C
|
B:ALA305
|
4.8
|
9.4
|
1.0
|
ND2
|
A:ASN271
|
4.8
|
9.8
|
1.0
|
CG
|
A:ASN271
|
4.9
|
16.5
|
1.0
|
O
|
A:SER52
|
4.9
|
8.8
|
1.0
|
|
Potassium binding site 2 out
of 4 in 1ax4
Go back to
Potassium Binding Sites List in 1ax4
Potassium binding site 2 out
of 4 in the Tryptophanase From Proteus Vulgaris
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Tryptophanase From Proteus Vulgaris within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K500
b:10.0
occ:1.00
|
O
|
A:HOH521
|
2.7
|
12.0
|
1.0
|
OE1
|
A:GLU70
|
2.7
|
9.2
|
1.0
|
O
|
B:HOH513
|
2.8
|
11.1
|
1.0
|
O
|
B:GLY53
|
2.9
|
7.2
|
1.0
|
O
|
B:HOH503
|
2.9
|
7.3
|
1.0
|
O
|
B:ASN271
|
3.0
|
10.4
|
1.0
|
O
|
A:GLU70
|
3.3
|
10.8
|
1.0
|
C
|
B:GLY53
|
3.7
|
13.5
|
1.0
|
CD
|
A:GLU70
|
3.9
|
20.6
|
1.0
|
C
|
B:ASN271
|
3.9
|
6.5
|
1.0
|
CB
|
A:GLU70
|
3.9
|
6.9
|
1.0
|
CA
|
B:GLY53
|
4.0
|
10.3
|
1.0
|
CB
|
B:ASN271
|
4.0
|
5.2
|
1.0
|
C
|
A:GLU70
|
4.1
|
8.7
|
1.0
|
CA
|
A:GLU70
|
4.1
|
5.1
|
1.0
|
CA
|
B:ASN271
|
4.2
|
4.9
|
1.0
|
CA
|
A:ALA305
|
4.3
|
10.5
|
1.0
|
N
|
A:GLY306
|
4.3
|
7.0
|
1.0
|
O
|
A:HOH502
|
4.4
|
6.7
|
1.0
|
CG
|
A:GLU70
|
4.5
|
10.4
|
1.0
|
ND2
|
B:ASN271
|
4.8
|
10.1
|
1.0
|
N
|
B:THR54
|
4.8
|
7.6
|
1.0
|
C
|
A:ALA305
|
4.8
|
8.7
|
1.0
|
OE2
|
A:GLU70
|
4.9
|
10.7
|
1.0
|
CE
|
B:LYS265
|
4.9
|
9.6
|
1.0
|
CG
|
B:ASN271
|
4.9
|
16.2
|
1.0
|
CB
|
A:ALA305
|
4.9
|
8.1
|
1.0
|
O
|
A:LEU304
|
4.9
|
11.7
|
1.0
|
O
|
B:SER52
|
5.0
|
8.6
|
1.0
|
|
Potassium binding site 3 out
of 4 in 1ax4
Go back to
Potassium Binding Sites List in 1ax4
Potassium binding site 3 out
of 4 in the Tryptophanase From Proteus Vulgaris
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Tryptophanase From Proteus Vulgaris within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K500
b:10.2
occ:1.00
|
OE1
|
D:GLU70
|
2.7
|
8.8
|
1.0
|
O
|
D:HOH509
|
2.7
|
10.4
|
1.0
|
O
|
C:HOH506
|
2.8
|
8.9
|
1.0
|
O
|
C:GLY53
|
2.8
|
7.0
|
1.0
|
O
|
C:ASN271
|
2.9
|
9.9
|
1.0
|
O
|
C:HOH529
|
3.0
|
13.8
|
1.0
|
O
|
D:GLU70
|
3.4
|
10.6
|
1.0
|
C
|
C:GLY53
|
3.6
|
13.5
|
1.0
|
CB
|
D:GLU70
|
3.8
|
6.8
|
1.0
|
CD
|
D:GLU70
|
3.8
|
20.2
|
1.0
|
CA
|
C:GLY53
|
3.9
|
10.0
|
1.0
|
C
|
C:ASN271
|
3.9
|
6.5
|
1.0
|
CB
|
C:ASN271
|
4.0
|
5.2
|
1.0
|
CA
|
D:GLU70
|
4.0
|
5.4
|
1.0
|
C
|
D:GLU70
|
4.1
|
8.6
|
1.0
|
CA
|
C:ASN271
|
4.2
|
4.9
|
1.0
|
O
|
D:HOH507
|
4.3
|
9.1
|
1.0
|
CA
|
D:ALA305
|
4.4
|
11.0
|
1.0
|
N
|
D:GLY306
|
4.4
|
7.2
|
1.0
|
CG
|
D:GLU70
|
4.4
|
10.2
|
1.0
|
N
|
C:THR54
|
4.7
|
7.4
|
1.0
|
CE
|
C:LYS265
|
4.8
|
8.8
|
1.0
|
OE2
|
D:GLU70
|
4.9
|
10.8
|
1.0
|
ND2
|
C:ASN271
|
4.9
|
10.0
|
1.0
|
O
|
C:SER52
|
4.9
|
8.4
|
1.0
|
C
|
D:ALA305
|
4.9
|
8.6
|
1.0
|
CG
|
C:ASN271
|
4.9
|
16.3
|
1.0
|
O
|
D:LEU304
|
4.9
|
12.3
|
1.0
|
CB
|
D:ALA305
|
5.0
|
7.9
|
1.0
|
|
Potassium binding site 4 out
of 4 in 1ax4
Go back to
Potassium Binding Sites List in 1ax4
Potassium binding site 4 out
of 4 in the Tryptophanase From Proteus Vulgaris
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Tryptophanase From Proteus Vulgaris within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K500
b:12.6
occ:1.00
|
OE1
|
C:GLU70
|
2.7
|
9.4
|
1.0
|
O
|
C:HOH511
|
2.8
|
9.9
|
1.0
|
O
|
C:HOH512
|
2.9
|
9.9
|
1.0
|
O
|
D:ASN271
|
2.9
|
10.4
|
1.0
|
O
|
D:GLY53
|
2.9
|
6.8
|
1.0
|
O
|
D:HOH517
|
3.0
|
13.1
|
1.0
|
O
|
C:GLU70
|
3.4
|
11.2
|
1.0
|
C
|
D:GLY53
|
3.6
|
13.5
|
1.0
|
C
|
D:ASN271
|
3.8
|
6.5
|
1.0
|
CD
|
C:GLU70
|
3.8
|
20.4
|
1.0
|
CA
|
D:GLY53
|
3.9
|
10.3
|
1.0
|
CB
|
C:GLU70
|
3.9
|
7.0
|
1.0
|
CB
|
D:ASN271
|
3.9
|
4.9
|
1.0
|
CA
|
D:ASN271
|
4.1
|
4.8
|
1.0
|
CA
|
C:GLU70
|
4.1
|
5.5
|
1.0
|
C
|
C:GLU70
|
4.2
|
8.7
|
1.0
|
CA
|
C:ALA305
|
4.3
|
10.6
|
1.0
|
N
|
C:GLY306
|
4.4
|
7.0
|
1.0
|
O
|
C:HOH504
|
4.4
|
8.0
|
1.0
|
CG
|
C:GLU70
|
4.5
|
10.0
|
1.0
|
N
|
D:THR54
|
4.8
|
7.6
|
1.0
|
ND2
|
D:ASN271
|
4.8
|
9.9
|
1.0
|
CE
|
D:LYS265
|
4.8
|
9.3
|
1.0
|
C
|
C:ALA305
|
4.8
|
8.6
|
1.0
|
OE2
|
C:GLU70
|
4.8
|
10.4
|
1.0
|
CG
|
D:ASN271
|
4.9
|
16.2
|
1.0
|
O
|
D:SER52
|
4.9
|
8.9
|
1.0
|
O
|
C:LEU304
|
4.9
|
11.7
|
1.0
|
CB
|
C:ALA305
|
4.9
|
8.2
|
1.0
|
|
Reference:
M.N.Isupov,
A.A.Antson,
E.J.Dodson,
G.G.Dodson,
I.S.Dementieva,
L.N.Zakomirdina,
K.S.Wilson,
Z.Dauter,
A.A.Lebedev,
E.H.Harutyunyan.
Crystal Structure of Tryptophanase. J.Mol.Biol. V. 276 603 1998.
ISSN: ISSN 0022-2836
PubMed: 9551100
DOI: 10.1006/JMBI.1997.1561
Page generated: Mon Aug 12 04:02:31 2024
|