Zinc in PDB 5vlc: Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol
Enzymatic activity of Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol
All present enzymatic activity of Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol:
1.1.1.23;
Protein crystallography data
The structure of Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol, PDB code: 5vlc
was solved by
M.Ruszkowski,
Z.Dauter,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.73 /
1.97
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
102.859,
139.201,
102.692,
90.00,
119.18,
90.00
|
R / Rfree (%)
|
17.9 /
22.9
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol
(pdb code 5vlc). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the
Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol, PDB code: 5vlc:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 5vlc
Go back to
Zinc Binding Sites List in 5vlc
Zinc binding site 1 out
of 6 in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn502
b:30.2
occ:1.00
|
OD2
|
B:ASP401
|
2.0
|
25.5
|
1.0
|
ND1
|
B:HSO502
|
2.1
|
29.0
|
1.0
|
OE1
|
B:GLN299
|
2.1
|
28.6
|
1.0
|
N
|
B:HSO502
|
2.1
|
28.9
|
1.0
|
NE2
|
B:HIS302
|
2.1
|
29.8
|
1.0
|
NE2
|
A:HIS460
|
2.1
|
28.6
|
1.0
|
CD
|
B:GLN299
|
3.0
|
30.0
|
1.0
|
CG
|
B:ASP401
|
3.0
|
28.5
|
1.0
|
CG
|
B:HSO502
|
3.0
|
29.5
|
1.0
|
CE1
|
B:HIS302
|
3.0
|
31.4
|
1.0
|
CE1
|
B:HSO502
|
3.1
|
29.7
|
1.0
|
CE1
|
A:HIS460
|
3.1
|
28.9
|
1.0
|
CD2
|
A:HIS460
|
3.1
|
28.5
|
1.0
|
CA
|
B:HSO502
|
3.1
|
30.2
|
1.0
|
CD2
|
B:HIS302
|
3.1
|
30.8
|
1.0
|
NE2
|
B:GLN299
|
3.3
|
31.7
|
1.0
|
CB
|
B:HSO502
|
3.4
|
29.6
|
1.0
|
OD1
|
B:ASP401
|
3.7
|
27.8
|
1.0
|
CB
|
B:ASP401
|
4.0
|
28.3
|
1.0
|
OE2
|
B:GLU397
|
4.0
|
31.1
|
1.0
|
CD2
|
B:HSO502
|
4.2
|
29.4
|
1.0
|
ND1
|
B:HIS302
|
4.2
|
32.7
|
1.0
|
NE2
|
B:HSO502
|
4.2
|
30.0
|
1.0
|
ND1
|
A:HIS460
|
4.2
|
29.9
|
1.0
|
CG
|
A:HIS460
|
4.3
|
29.6
|
1.0
|
CG
|
B:HIS302
|
4.3
|
32.7
|
1.0
|
CG
|
B:GLN299
|
4.5
|
30.1
|
1.0
|
C
|
B:HSO502
|
4.6
|
30.4
|
1.0
|
OG
|
B:SER277
|
4.6
|
44.6
|
1.0
|
O
|
B:SER298
|
4.9
|
31.9
|
1.0
|
|
Zinc binding site 2 out
of 6 in 5vlc
Go back to
Zinc Binding Sites List in 5vlc
Zinc binding site 2 out
of 6 in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn501
b:26.0
occ:1.00
|
OD2
|
A:ASP401
|
2.0
|
23.4
|
1.0
|
OE1
|
A:GLN299
|
2.1
|
26.4
|
1.0
|
N
|
A:HSO501
|
2.1
|
24.9
|
1.0
|
ND1
|
A:HSO501
|
2.1
|
24.3
|
1.0
|
NE2
|
B:HIS460
|
2.1
|
24.0
|
1.0
|
NE2
|
A:HIS302
|
2.1
|
25.6
|
1.0
|
CG
|
A:ASP401
|
3.0
|
25.4
|
1.0
|
CD
|
A:GLN299
|
3.0
|
27.6
|
1.0
|
CE1
|
A:HSO501
|
3.0
|
24.1
|
1.0
|
CE1
|
B:HIS460
|
3.0
|
24.4
|
1.0
|
CE1
|
A:HIS302
|
3.0
|
26.8
|
1.0
|
CG
|
A:HSO501
|
3.1
|
24.6
|
1.0
|
CD2
|
B:HIS460
|
3.1
|
24.1
|
1.0
|
CA
|
A:HSO501
|
3.1
|
25.6
|
1.0
|
CD2
|
A:HIS302
|
3.2
|
25.8
|
1.0
|
NE2
|
A:GLN299
|
3.3
|
29.2
|
1.0
|
CB
|
A:HSO501
|
3.5
|
24.8
|
1.0
|
OD1
|
A:ASP401
|
3.6
|
23.9
|
1.0
|
CB
|
A:ASP401
|
4.0
|
24.7
|
1.0
|
OE2
|
A:GLU397
|
4.1
|
29.3
|
1.0
|
CD2
|
A:HSO501
|
4.2
|
24.1
|
1.0
|
ND1
|
B:HIS460
|
4.2
|
24.4
|
1.0
|
NE2
|
A:HSO501
|
4.2
|
25.1
|
1.0
|
ND1
|
A:HIS302
|
4.2
|
27.4
|
1.0
|
CG
|
B:HIS460
|
4.2
|
24.9
|
1.0
|
CG
|
A:HIS302
|
4.3
|
26.7
|
1.0
|
CG
|
A:GLN299
|
4.5
|
26.7
|
1.0
|
C
|
A:HSO501
|
4.5
|
26.4
|
1.0
|
O
|
A:SER298
|
4.9
|
30.3
|
1.0
|
O
|
A:HSO501
|
5.0
|
30.5
|
1.0
|
CD
|
A:GLU397
|
5.0
|
29.1
|
1.0
|
|
Zinc binding site 3 out
of 6 in 5vlc
Go back to
Zinc Binding Sites List in 5vlc
Zinc binding site 3 out
of 6 in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn501
b:37.4
occ:1.00
|
OE1
|
C:GLN299
|
2.0
|
38.4
|
1.0
|
OD2
|
C:ASP401
|
2.1
|
35.8
|
1.0
|
N
|
C:HSO502
|
2.1
|
35.5
|
1.0
|
ND1
|
C:HSO502
|
2.1
|
37.0
|
1.0
|
NE2
|
D:HIS460
|
2.1
|
39.6
|
1.0
|
NE2
|
C:HIS302
|
2.1
|
37.7
|
1.0
|
CD
|
C:GLN299
|
3.0
|
38.9
|
1.0
|
CG
|
C:ASP401
|
3.0
|
35.1
|
1.0
|
CE1
|
D:HIS460
|
3.0
|
39.7
|
1.0
|
CE1
|
C:HIS302
|
3.0
|
38.4
|
1.0
|
CG
|
C:HSO502
|
3.1
|
37.0
|
1.0
|
CE1
|
C:HSO502
|
3.1
|
39.0
|
1.0
|
CA
|
C:HSO502
|
3.1
|
36.0
|
1.0
|
CD2
|
D:HIS460
|
3.2
|
38.7
|
1.0
|
CD2
|
C:HIS302
|
3.2
|
39.0
|
1.0
|
NE2
|
C:GLN299
|
3.3
|
39.9
|
1.0
|
CB
|
C:HSO502
|
3.5
|
36.0
|
1.0
|
OD1
|
C:ASP401
|
3.6
|
34.3
|
1.0
|
OE2
|
C:GLU397
|
4.0
|
36.5
|
1.0
|
CB
|
C:ASP401
|
4.0
|
34.1
|
1.0
|
ND1
|
D:HIS460
|
4.1
|
40.7
|
1.0
|
ND1
|
C:HIS302
|
4.2
|
37.6
|
1.0
|
CD2
|
C:HSO502
|
4.2
|
36.0
|
1.0
|
NE2
|
C:HSO502
|
4.3
|
37.6
|
1.0
|
CG
|
D:HIS460
|
4.3
|
40.2
|
1.0
|
CG
|
C:HIS302
|
4.3
|
39.0
|
1.0
|
CG
|
C:GLN299
|
4.4
|
39.7
|
1.0
|
C
|
C:HSO502
|
4.5
|
36.4
|
1.0
|
OG
|
C:SER277
|
4.6
|
45.6
|
1.0
|
O
|
C:SER298
|
4.8
|
41.2
|
1.0
|
CD
|
C:GLU397
|
4.9
|
37.0
|
1.0
|
O
|
C:HSO502
|
4.9
|
38.1
|
1.0
|
|
Zinc binding site 4 out
of 6 in 5vlc
Go back to
Zinc Binding Sites List in 5vlc
Zinc binding site 4 out
of 6 in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn501
b:39.1
occ:1.00
|
OE1
|
D:GLN299
|
2.1
|
39.6
|
1.0
|
OD2
|
D:ASP401
|
2.1
|
35.6
|
1.0
|
NE2
|
C:HIS460
|
2.1
|
41.4
|
1.0
|
ND1
|
D:HSO502
|
2.1
|
35.8
|
1.0
|
N
|
D:HSO502
|
2.1
|
36.1
|
1.0
|
NE2
|
D:HIS302
|
2.1
|
42.6
|
1.0
|
CE1
|
C:HIS460
|
2.9
|
43.8
|
1.0
|
CG
|
D:ASP401
|
3.0
|
35.4
|
1.0
|
CE1
|
D:HSO502
|
3.0
|
35.6
|
1.0
|
CE1
|
D:HIS302
|
3.0
|
43.6
|
1.0
|
CD
|
D:GLN299
|
3.1
|
39.6
|
1.0
|
CG
|
D:HSO502
|
3.1
|
36.5
|
1.0
|
CD2
|
D:HIS302
|
3.2
|
44.3
|
1.0
|
CD2
|
C:HIS460
|
3.2
|
42.3
|
1.0
|
CA
|
D:HSO502
|
3.2
|
36.3
|
1.0
|
NE2
|
D:GLN299
|
3.4
|
40.9
|
1.0
|
CB
|
D:HSO502
|
3.5
|
35.9
|
1.0
|
OD1
|
D:ASP401
|
3.6
|
35.5
|
1.0
|
CB
|
D:ASP401
|
4.0
|
34.9
|
1.0
|
ND1
|
C:HIS460
|
4.1
|
45.4
|
1.0
|
OE2
|
D:GLU397
|
4.1
|
44.4
|
1.0
|
NE2
|
D:HSO502
|
4.2
|
35.5
|
1.0
|
ND1
|
D:HIS302
|
4.2
|
44.9
|
1.0
|
CD2
|
D:HSO502
|
4.2
|
36.0
|
1.0
|
CG
|
C:HIS460
|
4.2
|
44.3
|
1.0
|
CG
|
D:HIS302
|
4.3
|
45.6
|
1.0
|
CG
|
D:GLN299
|
4.5
|
40.5
|
1.0
|
C
|
D:HSO502
|
4.5
|
38.5
|
1.0
|
O
|
D:SER298
|
4.9
|
44.6
|
1.0
|
OG
|
D:SER277
|
4.9
|
53.2
|
1.0
|
CA
|
D:GLN299
|
5.0
|
41.7
|
1.0
|
|
Zinc binding site 5 out
of 6 in 5vlc
Go back to
Zinc Binding Sites List in 5vlc
Zinc binding site 5 out
of 6 in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn501
b:45.5
occ:1.00
|
OE1
|
E:GLN299
|
2.0
|
38.6
|
1.0
|
OD2
|
E:ASP401
|
2.1
|
47.0
|
1.0
|
ND1
|
E:HSO502
|
2.1
|
44.4
|
1.0
|
NE2
|
F:HIS460
|
2.1
|
49.6
|
1.0
|
N
|
E:HSO502
|
2.1
|
44.6
|
1.0
|
NE2
|
E:HIS302
|
2.1
|
50.8
|
1.0
|
CE1
|
F:HIS460
|
2.9
|
49.4
|
1.0
|
CG
|
E:ASP401
|
3.0
|
44.6
|
1.0
|
CE1
|
E:HIS302
|
3.0
|
51.3
|
1.0
|
CD
|
E:GLN299
|
3.0
|
40.8
|
1.0
|
CG
|
E:HSO502
|
3.0
|
45.2
|
1.0
|
CA
|
E:HSO502
|
3.1
|
44.0
|
1.0
|
CE1
|
E:HSO502
|
3.1
|
44.4
|
1.0
|
CD2
|
E:HIS302
|
3.2
|
52.1
|
1.0
|
CD2
|
F:HIS460
|
3.3
|
49.6
|
1.0
|
NE2
|
E:GLN299
|
3.4
|
40.1
|
1.0
|
CB
|
E:HSO502
|
3.5
|
45.1
|
1.0
|
OD1
|
E:ASP401
|
3.5
|
44.2
|
1.0
|
OE2
|
E:GLU397
|
4.0
|
41.5
|
1.0
|
CB
|
E:ASP401
|
4.1
|
45.2
|
1.0
|
ND1
|
F:HIS460
|
4.1
|
50.3
|
1.0
|
ND1
|
E:HIS302
|
4.2
|
52.3
|
1.0
|
CD2
|
E:HSO502
|
4.2
|
45.9
|
1.0
|
NE2
|
E:HSO502
|
4.3
|
44.4
|
1.0
|
CG
|
F:HIS460
|
4.3
|
50.0
|
1.0
|
CG
|
E:HIS302
|
4.3
|
52.5
|
1.0
|
CG
|
E:GLN299
|
4.4
|
41.2
|
1.0
|
C
|
E:HSO502
|
4.5
|
45.1
|
1.0
|
O
|
E:SER298
|
4.8
|
45.7
|
1.0
|
OG
|
E:SER277
|
4.9
|
50.0
|
1.0
|
CD
|
E:GLU397
|
4.9
|
41.9
|
1.0
|
CA
|
E:GLN299
|
5.0
|
45.2
|
1.0
|
|
Zinc binding site 6 out
of 6 in 5vlc
Go back to
Zinc Binding Sites List in 5vlc
Zinc binding site 6 out
of 6 in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn503
b:46.3
occ:1.00
|
OE1
|
F:GLN299
|
2.0
|
43.0
|
1.0
|
OD2
|
F:ASP401
|
2.0
|
41.3
|
1.0
|
ND1
|
F:HSO501
|
2.1
|
48.8
|
1.0
|
NE2
|
F:HIS302
|
2.1
|
46.1
|
1.0
|
N
|
F:HSO501
|
2.1
|
47.2
|
1.0
|
NE2
|
E:HIS460
|
2.1
|
50.1
|
1.0
|
CD
|
F:GLN299
|
3.0
|
43.9
|
1.0
|
CG
|
F:ASP401
|
3.0
|
43.6
|
1.0
|
CE1
|
F:HIS302
|
3.0
|
47.2
|
1.0
|
CE1
|
E:HIS460
|
3.1
|
51.2
|
1.0
|
CE1
|
F:HSO501
|
3.1
|
50.4
|
1.0
|
CG
|
F:HSO501
|
3.1
|
49.0
|
1.0
|
CA
|
F:HSO501
|
3.1
|
48.2
|
1.0
|
CD2
|
F:HIS302
|
3.2
|
46.8
|
1.0
|
CD2
|
E:HIS460
|
3.2
|
50.0
|
1.0
|
NE2
|
F:GLN299
|
3.3
|
45.5
|
1.0
|
CB
|
F:HSO501
|
3.5
|
47.0
|
1.0
|
OD1
|
F:ASP401
|
3.7
|
39.8
|
1.0
|
CB
|
F:ASP401
|
4.0
|
43.0
|
1.0
|
OE2
|
F:GLU397
|
4.0
|
44.9
|
1.0
|
ND1
|
F:HIS302
|
4.2
|
46.8
|
1.0
|
CD2
|
F:HSO501
|
4.2
|
48.3
|
1.0
|
ND1
|
E:HIS460
|
4.2
|
52.0
|
1.0
|
NE2
|
F:HSO501
|
4.2
|
51.1
|
1.0
|
CG
|
F:HIS302
|
4.3
|
48.4
|
1.0
|
CG
|
E:HIS460
|
4.3
|
51.2
|
1.0
|
CG
|
F:GLN299
|
4.4
|
44.9
|
1.0
|
C
|
F:HSO501
|
4.5
|
48.4
|
1.0
|
CD
|
F:GLU397
|
4.8
|
44.0
|
1.0
|
OG
|
F:SER277
|
4.9
|
54.4
|
1.0
|
O
|
F:SER298
|
4.9
|
51.5
|
1.0
|
CB
|
F:GLN299
|
5.0
|
45.8
|
1.0
|
|
Reference:
M.Ruszkowski,
Z.Dauter.
Structures of Medicago Truncatula L-Histidinol Dehydrogenase Show Rearrangements Required For Nad(+) Binding and the Cofactor Positioned to Accept A Hydride. Sci Rep V. 7 10476 2017.
ISSN: ESSN 2045-2322
PubMed: 28874718
DOI: 10.1038/S41598-017-10859-0
Page generated: Mon Oct 28 13:04:03 2024
|