Manganese in PDB 1s5n: Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift
Enzymatic activity of Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift
All present enzymatic activity of Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift:
5.3.1.5;
Protein crystallography data
The structure of Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift, PDB code: 1s5n
was solved by
T.D.Fenn,
D.Ringe,
G.A.Petsko,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
0.95
|
Space group
|
I 2 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
86.031,
92.854,
98.312,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
10.6 /
12.8
|
Other elements in 1s5n:
The structure of Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift
(pdb code 1s5n). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the
Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift, PDB code: 1s5n:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 1s5n
Go back to
Manganese Binding Sites List in 1s5n
Manganese binding site 1 out
of 4 in the Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn2001
b:6.6
occ:0.95
|
HO2
|
A:XYL1001
|
1.7
|
11.2
|
1.0
|
HO4
|
A:XYL1001
|
1.7
|
10.3
|
1.0
|
OE1
|
A:GLU216
|
2.1
|
10.9
|
1.0
|
OD2
|
A:ASP244
|
2.1
|
8.5
|
1.0
|
OE2
|
A:GLU180
|
2.1
|
7.3
|
1.0
|
OD2
|
A:ASP286
|
2.1
|
10.0
|
1.0
|
O2
|
A:XYL1001
|
2.2
|
7.5
|
1.0
|
O4
|
A:XYL1001
|
2.3
|
6.8
|
1.0
|
CD
|
A:GLU180
|
3.0
|
6.5
|
1.0
|
HO
|
A:OH2006
|
3.2
|
21.6
|
1.0
|
CG
|
A:ASP286
|
3.2
|
6.8
|
1.0
|
CG
|
A:ASP244
|
3.3
|
6.7
|
1.0
|
CD
|
A:GLU216
|
3.3
|
7.3
|
1.0
|
OE1
|
A:GLU180
|
3.3
|
7.4
|
1.0
|
C2
|
A:XYL1001
|
3.3
|
7.4
|
1.0
|
C4
|
A:XYL1001
|
3.3
|
6.7
|
1.0
|
HB2
|
A:GLU216
|
3.4
|
6.7
|
1.0
|
HB3
|
A:ASP286
|
3.4
|
7.6
|
1.0
|
HO3
|
A:XYL1001
|
3.5
|
11.4
|
1.0
|
C3
|
A:XYL1001
|
3.5
|
7.2
|
1.0
|
H2
|
A:XYL1001
|
3.6
|
8.9
|
1.0
|
HE1
|
A:HIS219
|
3.6
|
15.7
|
1.0
|
HB3
|
A:ASP244
|
3.6
|
7.5
|
1.0
|
HB2
|
A:ASP286
|
3.7
|
7.6
|
1.0
|
CB
|
A:ASP286
|
3.7
|
6.3
|
1.0
|
H4
|
A:XYL1001
|
3.7
|
8.0
|
1.0
|
O3
|
A:XYL1001
|
3.7
|
7.6
|
1.0
|
MN
|
A:MN2002
|
3.8
|
6.3
|
0.1
|
HB2
|
A:ASP244
|
3.8
|
7.5
|
1.0
|
CB
|
A:ASP244
|
3.8
|
6.2
|
1.0
|
O
|
A:HOH2078
|
3.9
|
8.6
|
1.0
|
O
|
A:OH2006
|
3.9
|
14.4
|
1.0
|
CE1
|
A:HIS219
|
4.1
|
13.1
|
1.0
|
CB
|
A:GLU216
|
4.1
|
5.6
|
1.0
|
CG
|
A:GLU216
|
4.1
|
6.2
|
1.0
|
OE2
|
A:GLU216
|
4.2
|
9.8
|
1.0
|
OD1
|
A:ASP244
|
4.3
|
8.0
|
1.0
|
OD1
|
A:ASP286
|
4.3
|
7.9
|
1.0
|
HG3
|
A:GLU216
|
4.4
|
7.4
|
1.0
|
HD21
|
A:ASN214
|
4.4
|
9.0
|
1.0
|
NE2
|
A:HIS219
|
4.4
|
13.0
|
1.0
|
CG
|
A:GLU180
|
4.4
|
6.4
|
1.0
|
HB3
|
A:GLU216
|
4.4
|
6.7
|
1.0
|
H3
|
A:XYL1001
|
4.5
|
8.6
|
1.0
|
C1
|
A:XYL1001
|
4.6
|
8.5
|
1.0
|
C5
|
A:XYL1001
|
4.6
|
7.5
|
1.0
|
HD22
|
A:ASN214
|
4.6
|
9.0
|
1.0
|
HO1
|
A:XYL1001
|
4.6
|
15.8
|
1.0
|
HZ2
|
A:TRP15
|
4.6
|
8.9
|
1.0
|
HG3
|
A:GLU180
|
4.7
|
7.7
|
1.0
|
H51
|
A:XYL1001
|
4.7
|
9.0
|
1.0
|
HG2
|
A:GLU180
|
4.7
|
7.7
|
1.0
|
H11
|
A:XYL1001
|
4.7
|
10.2
|
1.0
|
ND2
|
A:ASN214
|
4.8
|
7.5
|
1.0
|
H52
|
A:XYL1001
|
4.8
|
9.0
|
1.0
|
MN
|
A:MN2002
|
4.8
|
6.2
|
0.3
|
MN
|
A:MN2002
|
4.9
|
6.0
|
0.3
|
ND1
|
A:HIS219
|
4.9
|
8.9
|
1.0
|
|
Manganese binding site 2 out
of 4 in 1s5n
Go back to
Manganese Binding Sites List in 1s5n
Manganese binding site 2 out
of 4 in the Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn2002
b:6.0
occ:0.31
|
MN
|
A:MN2002
|
0.0
|
6.0
|
0.3
|
MN
|
A:MN2002
|
0.9
|
6.2
|
0.3
|
OD2
|
A:ASP254
|
1.5
|
12.8
|
0.4
|
O
|
A:HOH2488
|
1.5
|
20.6
|
0.5
|
MN
|
A:MN2002
|
1.5
|
6.3
|
0.1
|
OE2
|
A:GLU216
|
2.0
|
9.8
|
1.0
|
OD2
|
A:ASP254
|
2.2
|
17.1
|
0.4
|
OD1
|
A:ASP254
|
2.2
|
17.1
|
0.4
|
CG
|
A:ASP254
|
2.2
|
13.4
|
0.4
|
OD1
|
A:ASP254
|
2.2
|
8.9
|
0.4
|
OD1
|
A:ASP256
|
2.4
|
13.2
|
0.7
|
O
|
A:OH2006
|
2.4
|
14.4
|
1.0
|
OD1
|
A:ASP256
|
2.4
|
13.9
|
0.3
|
CG
|
A:ASP254
|
2.5
|
10.6
|
0.4
|
O
|
A:HOH2488
|
2.5
|
18.7
|
0.5
|
HO1
|
A:XYL1001
|
2.7
|
15.8
|
1.0
|
NE2
|
A:HIS219
|
2.8
|
13.0
|
1.0
|
HO
|
A:OH2006
|
2.8
|
21.6
|
1.0
|
HD2
|
A:HIS219
|
3.0
|
11.0
|
1.0
|
HB2
|
A:ASP254
|
3.0
|
12.4
|
0.2
|
CD
|
A:GLU216
|
3.1
|
7.3
|
1.0
|
CD2
|
A:HIS219
|
3.2
|
9.2
|
1.0
|
CG
|
A:ASP256
|
3.3
|
13.1
|
0.3
|
HD21
|
A:ASN246
|
3.3
|
8.1
|
1.0
|
CG
|
A:ASP256
|
3.3
|
10.0
|
0.7
|
OD2
|
A:ASP256
|
3.5
|
22.8
|
0.3
|
OD2
|
A:ASP256
|
3.5
|
18.9
|
0.7
|
OE1
|
A:GLU216
|
3.5
|
10.9
|
1.0
|
O1
|
A:XYL1001
|
3.5
|
10.5
|
1.0
|
CB
|
A:ASP254
|
3.7
|
10.6
|
0.4
|
O2
|
A:XYL1001
|
3.7
|
7.5
|
1.0
|
OD2
|
A:ASP254
|
3.8
|
9.7
|
0.2
|
CB
|
A:ASP254
|
3.9
|
10.4
|
0.2
|
HE3
|
A:LYS182
|
3.9
|
8.0
|
1.0
|
HD22
|
A:ASN246
|
3.9
|
8.1
|
1.0
|
ND2
|
A:ASN246
|
4.0
|
6.7
|
1.0
|
CE1
|
A:HIS219
|
4.0
|
13.1
|
1.0
|
HB2
|
A:ASP254
|
4.0
|
12.8
|
0.4
|
CB
|
A:ASP254
|
4.0
|
10.6
|
0.4
|
O
|
A:HOH2027
|
4.1
|
9.8
|
1.0
|
HB3
|
A:ASP254
|
4.1
|
12.4
|
0.2
|
HO2
|
A:XYL1001
|
4.1
|
11.2
|
1.0
|
HB3
|
A:ASP254
|
4.2
|
12.8
|
0.4
|
H11
|
A:XYL1001
|
4.2
|
10.2
|
1.0
|
HG2
|
A:GLU216
|
4.2
|
7.4
|
1.0
|
HZ3
|
A:LYS182
|
4.3
|
13.5
|
1.0
|
CG
|
A:GLU216
|
4.3
|
6.2
|
1.0
|
CG
|
A:ASP254
|
4.3
|
10.3
|
0.2
|
HB3
|
A:ASP254
|
4.4
|
12.8
|
0.4
|
C1
|
A:XYL1001
|
4.4
|
8.5
|
1.0
|
HE1
|
A:HIS219
|
4.4
|
15.7
|
1.0
|
HB2
|
A:ASP254
|
4.4
|
12.8
|
0.4
|
CG
|
A:HIS219
|
4.5
|
7.1
|
1.0
|
HZ1
|
A:LYS182
|
4.5
|
13.5
|
1.0
|
HA
|
A:ASP256
|
4.6
|
9.2
|
0.3
|
H
|
A:ASP256
|
4.6
|
8.7
|
0.3
|
HA
|
A:ASP256
|
4.7
|
9.1
|
0.7
|
H
|
A:ASP256
|
4.7
|
8.3
|
0.7
|
C2
|
A:XYL1001
|
4.7
|
7.4
|
1.0
|
NZ
|
A:LYS182
|
4.7
|
9.0
|
1.0
|
CB
|
A:ASP256
|
4.7
|
9.2
|
0.3
|
CB
|
A:ASP256
|
4.7
|
8.9
|
0.7
|
CE
|
A:LYS182
|
4.7
|
6.7
|
1.0
|
HA
|
A:ASP254
|
4.8
|
11.7
|
0.4
|
CA
|
A:ASP254
|
4.8
|
9.7
|
0.4
|
ND1
|
A:HIS219
|
4.9
|
8.9
|
1.0
|
HA
|
A:ASP254
|
4.9
|
10.1
|
0.4
|
HA3
|
A:GLY218
|
4.9
|
6.9
|
1.0
|
HG3
|
A:GLU216
|
4.9
|
7.4
|
1.0
|
MN
|
A:MN2001
|
4.9
|
6.6
|
0.9
|
CA
|
A:ASP254
|
4.9
|
8.4
|
0.4
|
HZ2
|
A:LYS288
|
5.0
|
45.9
|
1.0
|
|
Manganese binding site 3 out
of 4 in 1s5n
Go back to
Manganese Binding Sites List in 1s5n
Manganese binding site 3 out
of 4 in the Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn2002
b:6.2
occ:0.30
|
MN
|
A:MN2002
|
0.0
|
6.2
|
0.3
|
MN
|
A:MN2002
|
0.9
|
6.0
|
0.3
|
O
|
A:HOH2488
|
1.7
|
20.6
|
0.5
|
OD1
|
A:ASP256
|
1.7
|
13.2
|
0.7
|
OD1
|
A:ASP256
|
1.8
|
13.9
|
0.3
|
MN
|
A:MN2002
|
1.9
|
6.3
|
0.1
|
O
|
A:OH2006
|
1.9
|
14.4
|
1.0
|
OD2
|
A:ASP254
|
2.0
|
12.8
|
0.4
|
OE2
|
A:GLU216
|
2.0
|
9.8
|
1.0
|
HO
|
A:OH2006
|
2.3
|
21.6
|
1.0
|
OD1
|
A:ASP254
|
2.5
|
17.1
|
0.4
|
CG
|
A:ASP256
|
2.6
|
13.1
|
0.3
|
CG
|
A:ASP256
|
2.6
|
10.0
|
0.7
|
OD2
|
A:ASP254
|
2.7
|
17.1
|
0.4
|
CG
|
A:ASP254
|
2.7
|
13.4
|
0.4
|
OD2
|
A:ASP256
|
2.8
|
22.8
|
0.3
|
OD1
|
A:ASP254
|
2.8
|
8.9
|
0.4
|
O
|
A:HOH2488
|
2.9
|
18.7
|
0.5
|
OD2
|
A:ASP256
|
2.9
|
18.9
|
0.7
|
HD21
|
A:ASN246
|
3.0
|
8.1
|
1.0
|
CG
|
A:ASP254
|
3.0
|
10.6
|
0.4
|
CD
|
A:GLU216
|
3.0
|
7.3
|
1.0
|
HO1
|
A:XYL1001
|
3.2
|
15.8
|
1.0
|
HD22
|
A:ASN246
|
3.3
|
8.1
|
1.0
|
OE1
|
A:GLU216
|
3.4
|
10.9
|
1.0
|
HB2
|
A:ASP254
|
3.5
|
12.4
|
0.2
|
NE2
|
A:HIS219
|
3.5
|
13.0
|
1.0
|
ND2
|
A:ASN246
|
3.5
|
6.7
|
1.0
|
HD2
|
A:HIS219
|
3.7
|
11.0
|
1.0
|
O2
|
A:XYL1001
|
3.8
|
7.5
|
1.0
|
O1
|
A:XYL1001
|
3.9
|
10.5
|
1.0
|
CD2
|
A:HIS219
|
4.0
|
9.2
|
1.0
|
CB
|
A:ASP256
|
4.0
|
9.2
|
0.3
|
CB
|
A:ASP256
|
4.0
|
8.9
|
0.7
|
HO2
|
A:XYL1001
|
4.0
|
11.2
|
1.0
|
HA
|
A:ASP256
|
4.1
|
9.2
|
0.3
|
HA
|
A:ASP256
|
4.1
|
9.1
|
0.7
|
O
|
A:HOH2027
|
4.1
|
9.8
|
1.0
|
H11
|
A:XYL1001
|
4.2
|
10.2
|
1.0
|
CB
|
A:ASP254
|
4.2
|
10.6
|
0.4
|
OD2
|
A:ASP254
|
4.3
|
9.7
|
0.2
|
O
|
A:ASP286
|
4.3
|
7.7
|
1.0
|
CG
|
A:GLU216
|
4.3
|
6.2
|
1.0
|
HG2
|
A:GLU216
|
4.4
|
7.4
|
1.0
|
H
|
A:ASP256
|
4.4
|
8.7
|
0.3
|
CB
|
A:ASP254
|
4.4
|
10.4
|
0.2
|
HB3
|
A:ASP256
|
4.4
|
10.7
|
0.7
|
H
|
A:ASP256
|
4.5
|
8.3
|
0.7
|
HZ2
|
A:LYS288
|
4.5
|
45.9
|
1.0
|
CA
|
A:ASP256
|
4.5
|
7.6
|
0.3
|
CB
|
A:ASP254
|
4.5
|
10.6
|
0.4
|
CA
|
A:ASP256
|
4.5
|
7.6
|
0.7
|
C1
|
A:XYL1001
|
4.5
|
8.5
|
1.0
|
HB3
|
A:ASP256
|
4.5
|
11.0
|
0.3
|
HB2
|
A:ASP256
|
4.6
|
11.0
|
0.3
|
CE1
|
A:HIS219
|
4.6
|
13.1
|
1.0
|
HB3
|
A:ASP254
|
4.6
|
12.8
|
0.4
|
HB2
|
A:ASP254
|
4.6
|
12.8
|
0.4
|
HB2
|
A:ASP256
|
4.7
|
10.7
|
0.7
|
N
|
A:ASP256
|
4.7
|
7.2
|
0.3
|
N
|
A:ASP256
|
4.7
|
7.0
|
0.7
|
OD2
|
A:ASP286
|
4.7
|
10.0
|
1.0
|
CG
|
A:ASP286
|
4.7
|
6.8
|
1.0
|
HB3
|
A:ASP254
|
4.7
|
12.8
|
0.4
|
HE3
|
A:LYS182
|
4.7
|
8.0
|
1.0
|
CG
|
A:ASN246
|
4.8
|
5.7
|
1.0
|
HB3
|
A:ASP254
|
4.8
|
12.4
|
0.2
|
HO3
|
A:XYL1001
|
4.8
|
11.4
|
1.0
|
C2
|
A:XYL1001
|
4.8
|
7.4
|
1.0
|
CG
|
A:ASP254
|
4.8
|
10.3
|
0.2
|
HG3
|
A:GLU216
|
4.8
|
7.4
|
1.0
|
MN
|
A:MN2001
|
4.8
|
6.6
|
0.9
|
HB3
|
A:ASP286
|
4.8
|
7.6
|
1.0
|
OD1
|
A:ASP286
|
4.9
|
7.9
|
1.0
|
HZ3
|
A:LYS182
|
4.9
|
13.5
|
1.0
|
HE1
|
A:HIS219
|
4.9
|
15.7
|
1.0
|
|
Manganese binding site 4 out
of 4 in 1s5n
Go back to
Manganese Binding Sites List in 1s5n
Manganese binding site 4 out
of 4 in the Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn2002
b:6.3
occ:0.06
|
MN
|
A:MN2002
|
0.0
|
6.3
|
0.1
|
MN
|
A:MN2002
|
1.5
|
6.0
|
0.3
|
HO1
|
A:XYL1001
|
1.7
|
15.8
|
1.0
|
MN
|
A:MN2002
|
1.9
|
6.2
|
0.3
|
O
|
A:OH2006
|
2.1
|
14.4
|
1.0
|
NE2
|
A:HIS219
|
2.1
|
13.0
|
1.0
|
HO
|
A:OH2006
|
2.2
|
21.6
|
1.0
|
OD2
|
A:ASP254
|
2.2
|
12.8
|
0.4
|
O2
|
A:XYL1001
|
2.3
|
7.5
|
1.0
|
OE2
|
A:GLU216
|
2.4
|
9.8
|
1.0
|
O1
|
A:XYL1001
|
2.5
|
10.5
|
1.0
|
OD2
|
A:ASP254
|
2.7
|
17.1
|
0.4
|
HO2
|
A:XYL1001
|
2.8
|
11.2
|
1.0
|
OE1
|
A:GLU216
|
2.9
|
10.9
|
1.0
|
CD
|
A:GLU216
|
2.9
|
7.3
|
1.0
|
CE1
|
A:HIS219
|
2.9
|
13.1
|
1.0
|
O
|
A:HOH2488
|
3.0
|
20.6
|
0.5
|
CD2
|
A:HIS219
|
3.1
|
9.2
|
1.0
|
HE1
|
A:HIS219
|
3.1
|
15.7
|
1.0
|
C1
|
A:XYL1001
|
3.1
|
8.5
|
1.0
|
H11
|
A:XYL1001
|
3.2
|
10.2
|
1.0
|
C2
|
A:XYL1001
|
3.2
|
7.4
|
1.0
|
HD2
|
A:HIS219
|
3.3
|
11.0
|
1.0
|
CG
|
A:ASP254
|
3.3
|
13.4
|
0.4
|
CG
|
A:ASP254
|
3.5
|
10.6
|
0.4
|
OD1
|
A:ASP254
|
3.6
|
8.9
|
0.4
|
OD1
|
A:ASP256
|
3.6
|
13.2
|
0.7
|
H2
|
A:XYL1001
|
3.7
|
8.9
|
1.0
|
OD1
|
A:ASP254
|
3.7
|
17.1
|
0.4
|
O
|
A:HOH2488
|
3.7
|
18.7
|
0.5
|
OD1
|
A:ASP256
|
3.7
|
13.9
|
0.3
|
HZ3
|
A:LYS182
|
3.7
|
13.5
|
1.0
|
MN
|
A:MN2001
|
3.8
|
6.6
|
0.9
|
HE3
|
A:LYS182
|
3.8
|
8.0
|
1.0
|
HO3
|
A:XYL1001
|
4.0
|
11.4
|
1.0
|
ND1
|
A:HIS219
|
4.1
|
8.9
|
1.0
|
H12
|
A:XYL1001
|
4.1
|
10.2
|
1.0
|
OD2
|
A:ASP256
|
4.1
|
22.8
|
0.3
|
CG
|
A:HIS219
|
4.1
|
7.1
|
1.0
|
HB2
|
A:ASP254
|
4.1
|
12.4
|
0.2
|
OD2
|
A:ASP286
|
4.2
|
10.0
|
1.0
|
HD2
|
A:LYS182
|
4.2
|
7.5
|
1.0
|
CG
|
A:GLU216
|
4.3
|
6.2
|
1.0
|
HD21
|
A:ASN246
|
4.3
|
8.1
|
1.0
|
OD2
|
A:ASP256
|
4.3
|
18.9
|
0.7
|
CG
|
A:ASP256
|
4.3
|
13.1
|
0.3
|
OD2
|
A:ASP254
|
4.3
|
9.7
|
0.2
|
CG
|
A:ASP256
|
4.4
|
10.0
|
0.7
|
OE2
|
A:GLU180
|
4.4
|
7.3
|
1.0
|
NZ
|
A:LYS182
|
4.4
|
9.0
|
1.0
|
CE
|
A:LYS182
|
4.5
|
6.7
|
1.0
|
C3
|
A:XYL1001
|
4.5
|
7.2
|
1.0
|
HZ1
|
A:LYS182
|
4.5
|
13.5
|
1.0
|
HG2
|
A:GLU216
|
4.5
|
7.4
|
1.0
|
HO4
|
A:XYL1001
|
4.6
|
10.3
|
1.0
|
HB3
|
A:GLU216
|
4.6
|
6.7
|
1.0
|
O3
|
A:XYL1001
|
4.7
|
7.6
|
1.0
|
CB
|
A:ASP254
|
4.7
|
10.6
|
0.4
|
HB2
|
A:ASP254
|
4.8
|
12.8
|
0.4
|
CG
|
A:ASP286
|
4.8
|
6.8
|
1.0
|
HD22
|
A:ASN246
|
4.8
|
8.1
|
1.0
|
HB2
|
A:GLU216
|
4.8
|
6.7
|
1.0
|
CD
|
A:LYS182
|
4.9
|
6.2
|
1.0
|
HD1
|
A:HIS219
|
4.9
|
10.7
|
1.0
|
CB
|
A:GLU216
|
4.9
|
5.6
|
1.0
|
ND2
|
A:ASN246
|
4.9
|
6.7
|
1.0
|
CB
|
A:ASP254
|
4.9
|
10.4
|
0.2
|
CB
|
A:ASP254
|
4.9
|
10.6
|
0.4
|
HG3
|
A:GLU216
|
4.9
|
7.4
|
1.0
|
HB3
|
A:ASP254
|
5.0
|
12.8
|
0.4
|
HB3
|
A:ASP254
|
5.0
|
12.4
|
0.2
|
|
Reference:
T.D.Fenn,
D.Ringe,
G.A.Petsko.
Xylose Isomerase in Substrate and Inhibitor Michaelis States: Atomic Resolution Studies of A Metal-Mediated Hydride Shift(,). Biochemistry V. 43 6464 2004.
ISSN: ISSN 0006-2960
PubMed: 15157080
DOI: 10.1021/BI049812O
Page generated: Sat Oct 5 12:23:21 2024
|