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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

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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

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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

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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

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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

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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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