Zinc in PDB 7nut: Crystal Structure of Human AMDHD2 in Complex with Zn and GLCN6P
Enzymatic activity of Crystal Structure of Human AMDHD2 in Complex with Zn and GLCN6P
All present enzymatic activity of Crystal Structure of Human AMDHD2 in Complex with Zn and GLCN6P:
3.5.1.25;
Protein crystallography data
The structure of Crystal Structure of Human AMDHD2 in Complex with Zn and GLCN6P, PDB code: 7nut
was solved by
S.Ruegenberg,
V.Kroef,
U.Baumann,
M.S.Denzel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.71 /
1.90
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
63.261,
161.449,
86.621,
90,
90,
90
|
R / Rfree (%)
|
18.5 /
21.3
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Human AMDHD2 in Complex with Zn and GLCN6P
(pdb code 7nut). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Crystal Structure of Human AMDHD2 in Complex with Zn and GLCN6P, PDB code: 7nut:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 7nut
Go back to
Zinc Binding Sites List in 7nut
Zinc binding site 1 out
of 2 in the Crystal Structure of Human AMDHD2 in Complex with Zn and GLCN6P
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 Human AMDHD2 in Complex with Zn and GLCN6P within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn502
b:32.4
occ:1.00
|
O
|
A:HOH602
|
1.8
|
38.2
|
1.0
|
OE1
|
A:GLU143
|
1.9
|
36.1
|
1.0
|
NE2
|
A:HIS211
|
2.0
|
30.0
|
1.0
|
NE2
|
A:HIS232
|
2.2
|
30.6
|
1.0
|
O
|
A:HOH684
|
2.3
|
45.1
|
1.0
|
CD
|
A:GLU143
|
2.7
|
35.7
|
1.0
|
HE2
|
A:HIS155
|
2.8
|
43.1
|
1.0
|
HN21
|
A:GLP501
|
2.9
|
41.7
|
1.0
|
CE1
|
A:HIS211
|
2.9
|
30.8
|
1.0
|
OE2
|
A:GLU143
|
3.0
|
38.1
|
1.0
|
HE1
|
A:HIS211
|
3.1
|
36.5
|
1.0
|
CD2
|
A:HIS211
|
3.1
|
28.7
|
1.0
|
CE1
|
A:HIS232
|
3.1
|
30.2
|
1.0
|
CD2
|
A:HIS232
|
3.1
|
29.0
|
1.0
|
H2
|
A:GLP501
|
3.3
|
37.7
|
1.0
|
HE1
|
A:HIS232
|
3.3
|
34.6
|
1.0
|
HD2
|
A:HIS232
|
3.3
|
30.5
|
1.0
|
HD2
|
A:HIS211
|
3.4
|
32.0
|
1.0
|
HE22
|
A:GLN71
|
3.5
|
49.4
|
1.0
|
N2
|
A:GLP501
|
3.6
|
34.7
|
1.0
|
HN22
|
A:GLP501
|
3.6
|
41.7
|
1.0
|
NE2
|
A:HIS155
|
3.6
|
34.0
|
1.0
|
HG22
|
A:THR231
|
3.7
|
36.5
|
1.0
|
C2
|
A:GLP501
|
3.9
|
31.3
|
1.0
|
HO3
|
A:GLP501
|
3.9
|
36.5
|
1.0
|
HG21
|
A:THR231
|
3.9
|
36.5
|
1.0
|
HE21
|
A:GLN71
|
3.9
|
49.4
|
1.0
|
O3
|
A:GLP501
|
4.0
|
30.3
|
1.0
|
NE2
|
A:GLN71
|
4.1
|
38.6
|
1.0
|
ND1
|
A:HIS211
|
4.1
|
30.2
|
1.0
|
CG
|
A:GLU143
|
4.1
|
35.2
|
1.0
|
CG
|
A:HIS211
|
4.2
|
29.8
|
1.0
|
ND1
|
A:HIS232
|
4.3
|
29.8
|
1.0
|
CG2
|
A:THR231
|
4.3
|
30.9
|
1.0
|
HD2
|
A:HIS155
|
4.3
|
41.1
|
1.0
|
CG
|
A:HIS232
|
4.3
|
29.5
|
1.0
|
HG2
|
A:GLU143
|
4.3
|
42.2
|
1.0
|
HG3
|
A:GLU143
|
4.4
|
42.2
|
1.0
|
CD2
|
A:HIS155
|
4.4
|
34.0
|
1.0
|
O
|
A:HOH614
|
4.5
|
43.1
|
1.0
|
HG23
|
A:THR231
|
4.6
|
36.5
|
1.0
|
C3
|
A:GLP501
|
4.6
|
30.4
|
1.0
|
CE1
|
A:HIS155
|
4.7
|
33.9
|
1.0
|
HE1
|
A:HIS155
|
4.8
|
41.9
|
1.0
|
HB3
|
A:ALA236
|
4.8
|
35.5
|
1.0
|
HD1
|
A:HIS211
|
4.9
|
33.9
|
1.0
|
OD2
|
A:ASP294
|
4.9
|
40.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 7nut
Go back to
Zinc Binding Sites List in 7nut
Zinc binding site 2 out
of 2 in the Crystal Structure of Human AMDHD2 in Complex with Zn and GLCN6P
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 Human AMDHD2 in Complex with Zn and GLCN6P within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn502
b:35.1
occ:1.00
|
OE2
|
B:GLU143
|
1.9
|
35.4
|
1.0
|
O
|
B:HOH610
|
2.0
|
45.6
|
1.0
|
NE2
|
B:HIS211
|
2.0
|
32.0
|
1.0
|
O
|
B:HOH601
|
2.1
|
45.8
|
1.0
|
NE2
|
B:HIS232
|
2.2
|
31.0
|
1.0
|
CD
|
B:GLU143
|
2.7
|
35.6
|
1.0
|
OE1
|
B:GLU143
|
2.9
|
37.1
|
1.0
|
CE1
|
B:HIS211
|
3.0
|
33.6
|
1.0
|
HE2
|
B:HIS155
|
3.0
|
48.5
|
1.0
|
CD2
|
B:HIS211
|
3.1
|
30.8
|
1.0
|
HE1
|
B:HIS211
|
3.1
|
46.9
|
1.0
|
H2
|
B:GLP501
|
3.2
|
64.1
|
1.0
|
CE1
|
B:HIS232
|
3.2
|
31.1
|
1.0
|
CD2
|
B:HIS232
|
3.2
|
30.1
|
1.0
|
HD2
|
B:HIS211
|
3.3
|
40.9
|
1.0
|
N2
|
B:GLP501
|
3.3
|
54.3
|
1.0
|
HE1
|
B:HIS232
|
3.3
|
38.1
|
1.0
|
HD2
|
B:HIS232
|
3.3
|
36.2
|
1.0
|
HE22
|
B:GLN71
|
3.4
|
46.0
|
1.0
|
HN21
|
B:GLP501
|
3.5
|
65.2
|
1.0
|
HO3
|
B:GLP501
|
3.6
|
62.0
|
1.0
|
C2
|
B:GLP501
|
3.7
|
53.4
|
1.0
|
HG22
|
B:THR231
|
3.8
|
37.8
|
1.0
|
NE2
|
B:HIS155
|
3.8
|
38.1
|
1.0
|
HE21
|
B:GLN71
|
3.8
|
46.0
|
1.0
|
O3
|
B:GLP501
|
3.9
|
51.5
|
1.0
|
NE2
|
B:GLN71
|
4.0
|
36.4
|
1.0
|
HN22
|
B:GLP501
|
4.0
|
65.2
|
1.0
|
HG21
|
B:THR231
|
4.0
|
37.8
|
1.0
|
CG
|
B:GLU143
|
4.1
|
33.9
|
1.0
|
ND1
|
B:HIS211
|
4.1
|
32.6
|
1.0
|
CG
|
B:HIS211
|
4.2
|
31.2
|
1.0
|
ND1
|
B:HIS232
|
4.3
|
29.9
|
1.0
|
O
|
B:HOH615
|
4.3
|
38.0
|
1.0
|
CG
|
B:HIS232
|
4.3
|
29.3
|
1.0
|
HG2
|
B:GLU143
|
4.3
|
41.5
|
1.0
|
CG2
|
B:THR231
|
4.4
|
31.8
|
1.0
|
HG3
|
B:GLU143
|
4.4
|
41.5
|
1.0
|
C3
|
B:GLP501
|
4.4
|
58.1
|
1.0
|
OD2
|
B:ASP294
|
4.5
|
42.8
|
1.0
|
HD2
|
B:HIS155
|
4.6
|
56.4
|
1.0
|
CD2
|
B:HIS155
|
4.6
|
41.2
|
1.0
|
HG23
|
B:THR231
|
4.7
|
37.8
|
1.0
|
HB3
|
B:ALA236
|
4.7
|
40.2
|
1.0
|
CE1
|
B:HIS155
|
4.8
|
38.8
|
1.0
|
H1
|
B:GLP501
|
4.8
|
67.9
|
1.0
|
HE1
|
B:HIS155
|
4.9
|
49.5
|
1.0
|
HD1
|
B:HIS211
|
4.9
|
42.1
|
1.0
|
C1
|
B:GLP501
|
4.9
|
56.5
|
1.0
|
|
Reference:
V.Kroef,
S.Ruegenberg,
M.Horn,
K.Allmeroth,
L.Ebert,
S.Bozkus,
S.Miethe,
B.Schermer,
U.Baumann,
M.S.Denzel.
GFAT2 and AMDHD2 Act in Tandem to Control the Hexosamine Biosynthetic Pathway To Be Published.
Page generated: Wed Oct 30 07:58:20 2024
|