Zinc in PDB 1d8w: L-Rhamnose Isomerase
Enzymatic activity of L-Rhamnose Isomerase
All present enzymatic activity of L-Rhamnose Isomerase:
5.3.1.14;
Protein crystallography data
The structure of L-Rhamnose Isomerase, PDB code: 1d8w
was solved by
I.P.Korndorfer,
B.W.Matthews,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
1.60
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
169.849,
163.104,
78.150,
90.00,
110.32,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Zinc Binding Sites:
The binding sites of Zinc atom in the L-Rhamnose Isomerase
(pdb code 1d8w). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
L-Rhamnose Isomerase, PDB code: 1d8w:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 1d8w
Go back to
Zinc Binding Sites List in 1d8w
Zinc binding site 1 out
of 4 in the L-Rhamnose Isomerase
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of L-Rhamnose Isomerase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn450
b:31.7
occ:0.70
|
OE2
|
A:GLU234
|
1.9
|
20.4
|
1.0
|
ND1
|
A:HIS294
|
2.0
|
23.0
|
1.0
|
OD2
|
A:ASP334
|
2.1
|
39.0
|
1.0
|
OD2
|
A:ASP267
|
2.2
|
38.6
|
1.0
|
CD
|
A:GLU234
|
2.7
|
18.2
|
1.0
|
OE1
|
A:GLU234
|
2.9
|
17.8
|
1.0
|
CG
|
A:HIS294
|
3.0
|
24.0
|
1.0
|
CE1
|
A:HIS294
|
3.0
|
25.5
|
1.0
|
CG
|
A:ASP267
|
3.2
|
32.2
|
1.0
|
CB
|
A:HIS294
|
3.2
|
18.5
|
1.0
|
CG
|
A:ASP334
|
3.3
|
31.6
|
1.0
|
CB
|
A:ASP267
|
3.4
|
31.2
|
1.0
|
CB
|
A:ASP334
|
3.7
|
18.4
|
1.0
|
NE2
|
A:HIS270
|
3.9
|
40.3
|
1.0
|
CG
|
A:GLU234
|
4.1
|
11.6
|
1.0
|
NE2
|
A:HIS294
|
4.1
|
26.0
|
1.0
|
CD2
|
A:HIS294
|
4.1
|
23.4
|
1.0
|
CE1
|
A:HIS270
|
4.2
|
41.4
|
1.0
|
OD1
|
A:ASP267
|
4.3
|
39.1
|
1.0
|
O
|
A:HOH643
|
4.3
|
42.8
|
1.0
|
OD1
|
A:ASP334
|
4.3
|
36.0
|
1.0
|
O
|
A:HOH663
|
4.4
|
37.9
|
1.0
|
SG
|
A:CYS265
|
4.4
|
18.7
|
1.0
|
CD2
|
A:HIS270
|
4.6
|
44.3
|
1.0
|
CA
|
A:ASP267
|
4.6
|
23.2
|
1.0
|
O
|
A:HOH662
|
4.7
|
49.0
|
1.0
|
CA
|
A:HIS294
|
4.8
|
17.6
|
1.0
|
ND1
|
A:HIS270
|
4.9
|
35.5
|
1.0
|
|
Zinc binding site 2 out
of 4 in 1d8w
Go back to
Zinc Binding Sites List in 1d8w
Zinc binding site 2 out
of 4 in the L-Rhamnose Isomerase
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of L-Rhamnose Isomerase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn450
b:26.0
occ:0.70
|
OE2
|
B:GLU234
|
1.9
|
19.2
|
1.0
|
ND1
|
B:HIS294
|
1.9
|
19.0
|
1.0
|
OD2
|
B:ASP267
|
2.0
|
43.6
|
1.0
|
OD2
|
B:ASP334
|
2.2
|
33.5
|
1.0
|
CD
|
B:GLU234
|
2.9
|
23.1
|
1.0
|
CG
|
B:HIS294
|
2.9
|
19.7
|
1.0
|
CE1
|
B:HIS294
|
3.0
|
21.0
|
1.0
|
CG
|
B:ASP267
|
3.1
|
59.3
|
1.0
|
CB
|
B:HIS294
|
3.1
|
15.0
|
1.0
|
OE1
|
B:GLU234
|
3.1
|
17.9
|
1.0
|
O
|
B:HOH708
|
3.1
|
45.5
|
1.0
|
CG
|
B:ASP334
|
3.2
|
25.9
|
1.0
|
CB
|
B:ASP267
|
3.4
|
24.8
|
1.0
|
CB
|
B:ASP334
|
3.5
|
19.6
|
1.0
|
O
|
B:HOH653
|
3.9
|
49.9
|
1.0
|
CD2
|
B:HIS294
|
4.1
|
17.6
|
1.0
|
NE2
|
B:HIS294
|
4.1
|
20.2
|
1.0
|
OD1
|
B:ASP267
|
4.2
|
28.0
|
1.0
|
CG
|
B:GLU234
|
4.2
|
13.7
|
1.0
|
NE2
|
B:HIS270
|
4.2
|
74.3
|
1.0
|
OD1
|
B:ASP334
|
4.2
|
30.3
|
1.0
|
SG
|
B:CYS265
|
4.3
|
19.3
|
1.0
|
CA
|
B:ASP267
|
4.5
|
16.2
|
1.0
|
CD2
|
B:HIS270
|
4.6
|
72.4
|
1.0
|
CA
|
B:HIS294
|
4.6
|
14.8
|
1.0
|
CE1
|
B:HIS270
|
4.7
|
69.5
|
1.0
|
O
|
B:HOH554
|
4.9
|
42.5
|
1.0
|
|
Zinc binding site 3 out
of 4 in 1d8w
Go back to
Zinc Binding Sites List in 1d8w
Zinc binding site 3 out
of 4 in the L-Rhamnose Isomerase
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of L-Rhamnose Isomerase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn450
b:40.4
occ:0.70
|
OE2
|
C:GLU234
|
1.8
|
20.0
|
1.0
|
OD2
|
C:ASP267
|
2.0
|
60.1
|
1.0
|
ND1
|
C:HIS294
|
2.1
|
25.1
|
1.0
|
OD2
|
C:ASP334
|
2.2
|
45.0
|
1.0
|
CD
|
C:GLU234
|
2.8
|
18.0
|
1.0
|
CG
|
C:HIS294
|
2.9
|
19.9
|
1.0
|
CB
|
C:HIS294
|
3.1
|
17.6
|
1.0
|
CG
|
C:ASP267
|
3.1
|
32.1
|
1.0
|
OE1
|
C:GLU234
|
3.1
|
21.6
|
1.0
|
CE1
|
C:HIS294
|
3.2
|
24.4
|
1.0
|
CG
|
C:ASP334
|
3.3
|
44.0
|
1.0
|
CB
|
C:ASP267
|
3.5
|
22.4
|
1.0
|
CB
|
C:ASP334
|
3.7
|
15.6
|
1.0
|
NE2
|
C:HIS270
|
3.9
|
63.9
|
1.0
|
CE1
|
C:HIS270
|
4.1
|
49.8
|
1.0
|
CG
|
C:GLU234
|
4.1
|
15.8
|
1.0
|
CD2
|
C:HIS294
|
4.1
|
18.5
|
1.0
|
OD1
|
C:ASP267
|
4.1
|
29.0
|
1.0
|
NE2
|
C:HIS294
|
4.2
|
23.3
|
1.0
|
O
|
C:HOH814
|
4.3
|
54.5
|
1.0
|
OD1
|
C:ASP334
|
4.3
|
38.8
|
1.0
|
SG
|
C:CYS265
|
4.4
|
19.3
|
1.0
|
CA
|
C:ASP267
|
4.6
|
15.8
|
1.0
|
CD2
|
C:HIS270
|
4.6
|
56.3
|
1.0
|
CA
|
C:HIS294
|
4.6
|
12.2
|
1.0
|
ND1
|
C:HIS270
|
4.8
|
63.0
|
1.0
|
|
Zinc binding site 4 out
of 4 in 1d8w
Go back to
Zinc Binding Sites List in 1d8w
Zinc binding site 4 out
of 4 in the L-Rhamnose Isomerase
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of L-Rhamnose Isomerase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn450
b:39.3
occ:0.70
|
OD2
|
D:ASP267
|
1.8
|
0.0
|
1.0
|
OE2
|
D:GLU234
|
2.1
|
24.1
|
1.0
|
ND1
|
D:HIS294
|
2.1
|
22.4
|
1.0
|
OD2
|
D:ASP334
|
2.1
|
46.0
|
1.0
|
CG
|
D:ASP267
|
2.9
|
43.2
|
1.0
|
CD
|
D:GLU234
|
2.9
|
27.1
|
1.0
|
CG
|
D:HIS294
|
3.0
|
24.9
|
1.0
|
OE1
|
D:GLU234
|
3.1
|
20.8
|
1.0
|
CE1
|
D:HIS294
|
3.1
|
21.2
|
1.0
|
CB
|
D:HIS294
|
3.2
|
18.8
|
1.0
|
CG
|
D:ASP334
|
3.3
|
49.1
|
1.0
|
CB
|
D:ASP267
|
3.5
|
24.9
|
1.0
|
CB
|
D:ASP334
|
3.8
|
20.5
|
1.0
|
OD1
|
D:ASP267
|
3.9
|
25.6
|
1.0
|
NE2
|
D:HIS270
|
4.1
|
51.5
|
1.0
|
O
|
D:HOH649
|
4.1
|
34.2
|
1.0
|
CD2
|
D:HIS294
|
4.2
|
26.2
|
1.0
|
NE2
|
D:HIS294
|
4.2
|
23.1
|
1.0
|
CG
|
D:GLU234
|
4.3
|
16.1
|
1.0
|
OD1
|
D:ASP334
|
4.3
|
37.2
|
1.0
|
CE1
|
D:HIS270
|
4.3
|
46.8
|
1.0
|
SG
|
D:CYS265
|
4.6
|
21.1
|
1.0
|
CA
|
D:ASP267
|
4.6
|
28.1
|
1.0
|
CD2
|
D:HIS270
|
4.6
|
54.1
|
1.0
|
CA
|
D:HIS294
|
4.7
|
15.0
|
1.0
|
ND1
|
D:HIS270
|
5.0
|
68.5
|
1.0
|
|
Reference:
I.P.Korndorfer,
W.D.Fessner,
B.W.Matthews.
The Structure of Rhamnose Isomerase From Escherichia Coli and Its Relation with Xylose Isomerase Illustrates A Change Between Inter and Intra-Subunit Complementation During Evolution. J.Mol.Biol. V. 300 917 2000.
ISSN: ISSN 0022-2836
PubMed: 10891278
DOI: 10.1006/JMBI.2000.3896
Page generated: Sat Oct 12 23:34:20 2024
|