Zinc in PDB 5vld: Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and Nad+
Enzymatic activity of Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and Nad+
All present enzymatic activity of Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and Nad+:
1.1.1.23;
Protein crystallography data
The structure of Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and Nad+, PDB code: 5vld
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)
|
48.89 /
2.59
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
103.654,
139.095,
103.558,
90.00,
119.47,
90.00
|
R / Rfree (%)
|
22.1 /
26.4
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and Nad+
(pdb code 5vld). 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-Histidine and Nad+, PDB code: 5vld:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 5vld
Go back to
Zinc Binding Sites List in 5vld
Zinc binding site 1 out
of 6 in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and Nad+
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-Histidine and Nad+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn503
b:25.6
occ:1.00
|
OD2
|
B:ASP401
|
2.0
|
22.9
|
1.0
|
N
|
B:HIS502
|
2.1
|
26.0
|
1.0
|
OE1
|
B:GLN299
|
2.1
|
27.1
|
1.0
|
NE2
|
A:HIS460
|
2.1
|
25.7
|
1.0
|
NE2
|
B:HIS302
|
2.1
|
27.6
|
1.0
|
ND1
|
B:HIS502
|
2.1
|
25.8
|
1.0
|
CE1
|
A:HIS460
|
2.9
|
25.6
|
1.0
|
CA
|
B:HIS502
|
3.0
|
26.2
|
1.0
|
CG
|
B:ASP401
|
3.0
|
21.8
|
1.0
|
CE1
|
B:HIS302
|
3.0
|
28.2
|
1.0
|
CE1
|
B:HIS502
|
3.0
|
25.9
|
1.0
|
CD
|
B:GLN299
|
3.1
|
28.1
|
1.0
|
CG
|
B:HIS502
|
3.1
|
25.7
|
1.0
|
CD2
|
B:HIS302
|
3.1
|
28.2
|
1.0
|
CD2
|
A:HIS460
|
3.1
|
25.4
|
1.0
|
CB
|
B:HIS502
|
3.4
|
25.8
|
1.0
|
NE2
|
B:GLN299
|
3.4
|
28.1
|
1.0
|
OD1
|
B:ASP401
|
3.6
|
21.8
|
1.0
|
CB
|
B:ASP401
|
4.0
|
21.5
|
1.0
|
ND1
|
A:HIS460
|
4.1
|
25.5
|
1.0
|
NE2
|
B:HIS502
|
4.1
|
26.0
|
1.0
|
ND1
|
B:HIS302
|
4.1
|
28.9
|
1.0
|
CD2
|
B:HIS502
|
4.2
|
25.7
|
1.0
|
CG
|
A:HIS460
|
4.2
|
25.3
|
1.0
|
OE2
|
B:GLU397
|
4.2
|
22.3
|
1.0
|
CG
|
B:HIS302
|
4.2
|
28.8
|
1.0
|
C
|
B:HIS502
|
4.3
|
26.9
|
1.0
|
CG
|
B:GLN299
|
4.5
|
28.9
|
1.0
|
O
|
B:SER298
|
4.7
|
29.2
|
1.0
|
OG
|
B:SER277
|
4.8
|
35.1
|
1.0
|
OXT
|
B:HIS502
|
4.9
|
26.3
|
1.0
|
|
Zinc binding site 2 out
of 6 in 5vld
Go back to
Zinc Binding Sites List in 5vld
Zinc binding site 2 out
of 6 in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and Nad+
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-Histidine and Nad+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn501
b:30.5
occ:1.00
|
OD2
|
A:ASP401
|
2.0
|
27.9
|
1.0
|
OE1
|
A:GLN299
|
2.1
|
29.9
|
1.0
|
NE2
|
B:HIS460
|
2.1
|
33.3
|
1.0
|
N
|
A:HIS501
|
2.1
|
28.6
|
1.0
|
ND1
|
A:HIS501
|
2.1
|
28.7
|
1.0
|
NE2
|
A:HIS302
|
2.1
|
32.5
|
1.0
|
CG
|
A:ASP401
|
3.0
|
27.1
|
1.0
|
CE1
|
B:HIS460
|
3.0
|
33.8
|
1.0
|
CE1
|
A:HIS501
|
3.0
|
28.8
|
1.0
|
CE1
|
A:HIS302
|
3.0
|
33.1
|
1.0
|
CG
|
A:HIS501
|
3.1
|
28.0
|
1.0
|
CD
|
A:GLN299
|
3.1
|
29.9
|
1.0
|
CA
|
A:HIS501
|
3.1
|
27.9
|
1.0
|
CD2
|
B:HIS460
|
3.1
|
34.1
|
1.0
|
CD2
|
A:HIS302
|
3.2
|
32.9
|
1.0
|
NE2
|
A:GLN299
|
3.4
|
29.9
|
1.0
|
CB
|
A:HIS501
|
3.4
|
27.6
|
1.0
|
OD1
|
A:ASP401
|
3.6
|
27.2
|
1.0
|
CB
|
A:ASP401
|
4.0
|
27.0
|
1.0
|
NE2
|
A:HIS501
|
4.1
|
28.5
|
1.0
|
ND1
|
B:HIS460
|
4.1
|
34.5
|
1.0
|
CD2
|
A:HIS501
|
4.1
|
28.2
|
1.0
|
ND1
|
A:HIS302
|
4.2
|
33.6
|
1.0
|
CG
|
B:HIS460
|
4.2
|
34.6
|
1.0
|
OE2
|
A:GLU397
|
4.2
|
27.4
|
1.0
|
CG
|
A:HIS302
|
4.3
|
33.3
|
1.0
|
C
|
A:HIS501
|
4.4
|
27.4
|
1.0
|
CG
|
A:GLN299
|
4.5
|
30.2
|
1.0
|
O
|
A:SER298
|
4.7
|
30.9
|
1.0
|
OG
|
A:SER277
|
4.8
|
26.4
|
1.0
|
OXT
|
A:HIS501
|
5.0
|
27.2
|
1.0
|
|
Zinc binding site 3 out
of 6 in 5vld
Go back to
Zinc Binding Sites List in 5vld
Zinc binding site 3 out
of 6 in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and Nad+
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-Histidine and Nad+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn501
b:79.0
occ:1.00
|
OE1
|
C:GLN299
|
2.0
|
75.4
|
1.0
|
OD2
|
C:ASP401
|
2.0
|
74.1
|
1.0
|
N
|
C:HIS502
|
2.1
|
75.2
|
1.0
|
ND1
|
C:HIS502
|
2.1
|
79.6
|
1.0
|
NE2
|
C:HIS302
|
2.1
|
78.9
|
1.0
|
NE2
|
D:HIS460
|
2.2
|
66.6
|
1.0
|
CA
|
C:HIS502
|
2.9
|
74.8
|
1.0
|
CD
|
C:GLN299
|
3.0
|
74.6
|
1.0
|
CG
|
C:HIS502
|
3.0
|
78.3
|
1.0
|
CE1
|
C:HIS302
|
3.0
|
80.3
|
1.0
|
CG
|
C:ASP401
|
3.0
|
70.8
|
1.0
|
CE1
|
D:HIS460
|
3.0
|
69.1
|
1.0
|
CE1
|
C:HIS502
|
3.1
|
81.9
|
1.0
|
CD2
|
C:HIS302
|
3.2
|
79.1
|
1.0
|
CD2
|
D:HIS460
|
3.2
|
69.8
|
1.0
|
CB
|
C:HIS502
|
3.3
|
75.3
|
1.0
|
NE2
|
C:GLN299
|
3.3
|
75.0
|
1.0
|
OD1
|
C:ASP401
|
3.7
|
68.9
|
1.0
|
CB
|
C:ASP401
|
4.1
|
71.5
|
1.0
|
CD2
|
C:HIS502
|
4.1
|
79.6
|
1.0
|
NE2
|
C:HIS502
|
4.1
|
82.0
|
1.0
|
ND1
|
C:HIS302
|
4.2
|
82.0
|
1.0
|
ND1
|
D:HIS460
|
4.2
|
71.5
|
1.0
|
OE2
|
C:GLU397
|
4.2
|
62.2
|
1.0
|
CG
|
C:HIS302
|
4.3
|
81.0
|
1.0
|
C
|
C:HIS502
|
4.3
|
72.1
|
1.0
|
CG
|
D:HIS460
|
4.3
|
72.6
|
1.0
|
CG
|
C:GLN299
|
4.4
|
73.8
|
1.0
|
O
|
C:SER298
|
4.5
|
81.2
|
1.0
|
O
|
C:HIS502
|
4.9
|
71.5
|
1.0
|
OG
|
C:SER277
|
5.0
|
66.7
|
1.0
|
|
Zinc binding site 4 out
of 6 in 5vld
Go back to
Zinc Binding Sites List in 5vld
Zinc binding site 4 out
of 6 in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and Nad+
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-Histidine and Nad+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn501
b:68.2
occ:1.00
|
OD2
|
D:ASP401
|
2.0
|
67.6
|
1.0
|
OE1
|
D:GLN299
|
2.0
|
68.3
|
1.0
|
NE2
|
C:HIS460
|
2.1
|
0.8
|
1.0
|
ND1
|
D:HIS502
|
2.1
|
72.1
|
1.0
|
N
|
D:HIS502
|
2.1
|
69.0
|
1.0
|
NE2
|
D:HIS302
|
2.1
|
71.0
|
1.0
|
CE1
|
C:HIS460
|
2.8
|
0.8
|
1.0
|
CG
|
D:HIS502
|
3.0
|
72.2
|
1.0
|
CE1
|
D:HIS502
|
3.0
|
75.1
|
1.0
|
CE1
|
D:HIS302
|
3.0
|
70.7
|
1.0
|
CG
|
D:ASP401
|
3.0
|
64.9
|
1.0
|
CD
|
D:GLN299
|
3.0
|
67.8
|
1.0
|
CA
|
D:HIS502
|
3.1
|
69.2
|
1.0
|
CD2
|
C:HIS460
|
3.2
|
0.1
|
1.0
|
CD2
|
D:HIS302
|
3.2
|
70.6
|
1.0
|
CB
|
D:HIS502
|
3.4
|
69.5
|
1.0
|
NE2
|
D:GLN299
|
3.4
|
67.2
|
1.0
|
OD1
|
D:ASP401
|
3.7
|
64.3
|
1.0
|
ND1
|
C:HIS460
|
4.0
|
0.2
|
1.0
|
CB
|
D:ASP401
|
4.0
|
63.8
|
1.0
|
NE2
|
D:HIS502
|
4.1
|
75.6
|
1.0
|
CD2
|
D:HIS502
|
4.1
|
73.3
|
1.0
|
ND1
|
D:HIS302
|
4.2
|
73.0
|
1.0
|
CG
|
C:HIS460
|
4.2
|
0.6
|
1.0
|
CG
|
D:HIS302
|
4.3
|
72.9
|
1.0
|
OE2
|
D:GLU397
|
4.3
|
56.9
|
1.0
|
C
|
D:HIS502
|
4.3
|
71.0
|
1.0
|
CG
|
D:GLN299
|
4.5
|
68.8
|
1.0
|
O
|
D:SER298
|
4.5
|
71.6
|
1.0
|
OXT
|
D:HIS502
|
4.9
|
74.5
|
1.0
|
OG
|
D:SER277
|
5.0
|
70.2
|
1.0
|
|
Zinc binding site 5 out
of 6 in 5vld
Go back to
Zinc Binding Sites List in 5vld
Zinc binding site 5 out
of 6 in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and Nad+
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-Histidine and Nad+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn501
b:37.5
occ:1.00
|
OE1
|
E:GLN299
|
2.0
|
37.3
|
1.0
|
OD2
|
E:ASP401
|
2.0
|
34.9
|
1.0
|
NE2
|
E:HIS302
|
2.1
|
37.2
|
1.0
|
ND1
|
E:HIS502
|
2.1
|
35.5
|
1.0
|
NE2
|
F:HIS460
|
2.1
|
37.0
|
1.0
|
N
|
E:HIS502
|
2.1
|
34.8
|
1.0
|
CE1
|
F:HIS460
|
3.0
|
37.6
|
1.0
|
CG
|
E:ASP401
|
3.0
|
33.1
|
1.0
|
CE1
|
E:HIS302
|
3.0
|
37.2
|
1.0
|
CD
|
E:GLN299
|
3.0
|
37.3
|
1.0
|
CA
|
E:HIS502
|
3.0
|
33.7
|
1.0
|
CG
|
E:HIS502
|
3.1
|
35.1
|
1.0
|
CE1
|
E:HIS502
|
3.1
|
36.0
|
1.0
|
CD2
|
E:HIS302
|
3.1
|
37.6
|
1.0
|
CD2
|
F:HIS460
|
3.2
|
38.3
|
1.0
|
CB
|
E:HIS502
|
3.4
|
34.5
|
1.0
|
NE2
|
E:GLN299
|
3.4
|
36.9
|
1.0
|
OD1
|
E:ASP401
|
3.6
|
32.7
|
1.0
|
CB
|
E:ASP401
|
4.0
|
33.1
|
1.0
|
ND1
|
F:HIS460
|
4.1
|
39.0
|
1.0
|
ND1
|
E:HIS302
|
4.1
|
38.1
|
1.0
|
NE2
|
E:HIS502
|
4.2
|
36.3
|
1.0
|
CD2
|
E:HIS502
|
4.2
|
35.4
|
1.0
|
OE2
|
E:GLU397
|
4.2
|
32.3
|
1.0
|
CG
|
E:HIS302
|
4.2
|
38.6
|
1.0
|
CG
|
F:HIS460
|
4.2
|
40.2
|
1.0
|
C
|
E:HIS502
|
4.4
|
33.1
|
1.0
|
CG
|
E:GLN299
|
4.4
|
37.4
|
1.0
|
O
|
E:SER298
|
4.6
|
40.5
|
1.0
|
OG
|
E:SER277
|
4.8
|
34.3
|
1.0
|
O
|
E:HIS502
|
5.0
|
32.4
|
1.0
|
|
Zinc binding site 6 out
of 6 in 5vld
Go back to
Zinc Binding Sites List in 5vld
Zinc binding site 6 out
of 6 in the Crystal Structure of Medicago Truncatula L-Histidinol Dehydrogenase in Complex with L-Histidine and Nad+
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-Histidine and Nad+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn504
b:48.3
occ:1.00
|
OD2
|
F:ASP401
|
2.0
|
47.9
|
1.0
|
OE1
|
F:GLN299
|
2.1
|
44.9
|
1.0
|
NE2
|
E:HIS460
|
2.1
|
54.8
|
1.0
|
N
|
F:HIS501
|
2.1
|
43.7
|
1.0
|
NE2
|
F:HIS302
|
2.1
|
46.2
|
1.0
|
ND1
|
F:HIS501
|
2.3
|
45.7
|
1.0
|
CE1
|
E:HIS460
|
2.9
|
55.1
|
1.0
|
CG
|
F:ASP401
|
3.0
|
47.6
|
1.0
|
CE1
|
F:HIS302
|
3.0
|
46.0
|
1.0
|
CD
|
F:GLN299
|
3.1
|
45.1
|
1.0
|
CA
|
F:HIS501
|
3.1
|
43.0
|
1.0
|
CD2
|
E:HIS460
|
3.1
|
55.8
|
1.0
|
CD2
|
F:HIS302
|
3.2
|
45.5
|
1.0
|
CE1
|
F:HIS501
|
3.2
|
47.0
|
1.0
|
CG
|
F:HIS501
|
3.3
|
44.6
|
1.0
|
NE2
|
F:GLN299
|
3.4
|
46.3
|
1.0
|
CB
|
F:HIS501
|
3.6
|
43.5
|
1.0
|
OD1
|
F:ASP401
|
3.6
|
48.3
|
1.0
|
CB
|
F:ASP401
|
4.0
|
47.2
|
1.0
|
ND1
|
E:HIS460
|
4.1
|
56.2
|
1.0
|
ND1
|
F:HIS302
|
4.2
|
46.0
|
1.0
|
CG
|
E:HIS460
|
4.2
|
56.9
|
1.0
|
OE2
|
F:GLU397
|
4.2
|
41.7
|
1.0
|
CG
|
F:HIS302
|
4.3
|
46.0
|
1.0
|
NE2
|
F:HIS501
|
4.3
|
46.6
|
1.0
|
CD2
|
F:HIS501
|
4.3
|
45.5
|
1.0
|
C
|
F:HIS501
|
4.4
|
42.0
|
1.0
|
CG
|
F:GLN299
|
4.5
|
45.3
|
1.0
|
O
|
F:SER298
|
4.6
|
46.8
|
1.0
|
OG
|
F:SER277
|
4.9
|
41.9
|
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 13:05:18 2024
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