Zinc in PDB 7nuu: Crystal Structure of Human AMDHD2 in Complex with Zn
Enzymatic activity of Crystal Structure of Human AMDHD2 in Complex with Zn
All present enzymatic activity of Crystal Structure of Human AMDHD2 in Complex with Zn:
3.5.1.25;
Protein crystallography data
The structure of Crystal Structure of Human AMDHD2 in Complex with Zn, PDB code: 7nuu
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)
|
77.08 /
1.84
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
61.777,
84.336,
154.166,
90,
90,
90
|
R / Rfree (%)
|
18.2 /
20.6
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Human AMDHD2 in Complex with Zn
(pdb code 7nuu). 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, PDB code: 7nuu:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 7nuu
Go back to
Zinc Binding Sites List in 7nuu
Zinc binding site 1 out
of 2 in the Crystal Structure of Human AMDHD2 in Complex with Zn
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 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn501
b:24.3
occ:1.00
|
H31
|
A:GOL502
|
1.9
|
46.8
|
1.0
|
OE1
|
A:GLU143
|
1.9
|
28.8
|
1.0
|
NE2
|
A:HIS211
|
2.0
|
27.1
|
1.0
|
NE2
|
A:HIS232
|
2.1
|
26.9
|
1.0
|
O3
|
A:GOL502
|
2.3
|
41.9
|
1.0
|
C3
|
A:GOL502
|
2.3
|
39.0
|
1.0
|
O2
|
A:GOL502
|
2.5
|
37.0
|
1.0
|
CD
|
A:GLU143
|
2.8
|
27.4
|
1.0
|
C2
|
A:GOL502
|
2.8
|
40.8
|
1.0
|
CE1
|
A:HIS211
|
2.9
|
26.3
|
1.0
|
CE1
|
A:HIS232
|
3.0
|
25.6
|
1.0
|
HE1
|
A:HIS211
|
3.1
|
32.4
|
1.0
|
CD2
|
A:HIS211
|
3.1
|
25.7
|
1.0
|
CD2
|
A:HIS232
|
3.1
|
25.0
|
1.0
|
H2
|
A:GOL502
|
3.1
|
49.0
|
1.0
|
OE2
|
A:GLU143
|
3.2
|
28.1
|
1.0
|
HE1
|
A:HIS232
|
3.2
|
30.4
|
1.0
|
H32
|
A:GOL502
|
3.2
|
46.8
|
1.0
|
HO2
|
A:GOL502
|
3.3
|
37.0
|
1.0
|
HE22
|
A:GLN71
|
3.3
|
32.7
|
1.0
|
HD2
|
A:HIS232
|
3.3
|
29.8
|
1.0
|
HD2
|
A:HIS211
|
3.3
|
31.4
|
1.0
|
HG22
|
A:THR231
|
3.7
|
31.2
|
1.0
|
HE21
|
A:GLN71
|
3.8
|
32.7
|
1.0
|
NE2
|
A:HIS155
|
3.8
|
28.2
|
1.0
|
NE2
|
A:GLN71
|
3.9
|
26.9
|
1.0
|
HG21
|
A:THR231
|
3.9
|
31.2
|
1.0
|
ND1
|
A:HIS211
|
4.1
|
26.0
|
1.0
|
CG
|
A:GLU143
|
4.1
|
26.4
|
1.0
|
ND1
|
A:HIS232
|
4.1
|
24.7
|
1.0
|
CG
|
A:HIS211
|
4.2
|
25.6
|
1.0
|
O
|
A:HOH601
|
4.2
|
39.0
|
1.0
|
CG
|
A:HIS232
|
4.2
|
24.1
|
1.0
|
C1
|
A:GOL502
|
4.2
|
48.7
|
1.0
|
CG2
|
A:THR231
|
4.2
|
26.0
|
1.0
|
HG2
|
A:GLU143
|
4.3
|
31.4
|
1.0
|
HG3
|
A:GLU143
|
4.3
|
31.4
|
1.0
|
H11
|
A:GOL502
|
4.4
|
58.4
|
1.0
|
O
|
A:HOH647
|
4.5
|
27.0
|
1.0
|
HG23
|
A:THR231
|
4.5
|
31.2
|
1.0
|
HD2
|
A:HIS155
|
4.6
|
32.9
|
1.0
|
CD2
|
A:HIS155
|
4.6
|
28.3
|
1.0
|
HB3
|
A:ALA236
|
4.8
|
32.4
|
1.0
|
CE1
|
A:HIS155
|
4.8
|
28.2
|
1.0
|
H12
|
A:GOL502
|
4.8
|
58.4
|
1.0
|
HD1
|
A:HIS211
|
4.8
|
31.5
|
1.0
|
HE1
|
A:HIS155
|
4.9
|
32.6
|
1.0
|
HD1
|
A:HIS232
|
4.9
|
29.2
|
1.0
|
OD1
|
A:ASP294
|
4.9
|
29.1
|
1.0
|
O1
|
A:GOL502
|
5.0
|
53.6
|
1.0
|
|
Zinc binding site 2 out
of 2 in 7nuu
Go back to
Zinc Binding Sites List in 7nuu
Zinc binding site 2 out
of 2 in the Crystal Structure of Human AMDHD2 in Complex with Zn
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 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn501
b:26.9
occ:1.00
|
OE1
|
B:GLU143
|
1.9
|
31.0
|
1.0
|
O2
|
B:GOL502
|
1.9
|
37.0
|
1.0
|
NE2
|
B:HIS211
|
2.0
|
31.0
|
1.0
|
H11
|
B:GOL502
|
2.2
|
56.1
|
1.0
|
NE2
|
B:HIS232
|
2.2
|
30.6
|
1.0
|
C1
|
B:GOL502
|
2.5
|
46.8
|
1.0
|
O1
|
B:GOL502
|
2.5
|
46.3
|
1.0
|
C2
|
B:GOL502
|
2.7
|
44.1
|
1.0
|
CD
|
B:GLU143
|
2.8
|
30.0
|
1.0
|
CE1
|
B:HIS211
|
3.0
|
29.9
|
1.0
|
HE2
|
B:HIS155
|
3.1
|
37.6
|
1.0
|
CD2
|
B:HIS232
|
3.1
|
28.3
|
1.0
|
CD2
|
B:HIS211
|
3.1
|
29.4
|
1.0
|
OE2
|
B:GLU143
|
3.1
|
30.6
|
1.0
|
HE1
|
B:HIS211
|
3.1
|
36.5
|
1.0
|
HD2
|
B:HIS232
|
3.2
|
35.5
|
1.0
|
CE1
|
B:HIS232
|
3.2
|
28.7
|
1.0
|
HD2
|
B:HIS211
|
3.3
|
36.1
|
1.0
|
H2
|
B:GOL502
|
3.3
|
53.0
|
1.0
|
HO1
|
B:GOL502
|
3.3
|
55.6
|
1.0
|
HE22
|
B:GLN71
|
3.3
|
32.4
|
1.0
|
HE1
|
B:HIS232
|
3.4
|
35.9
|
1.0
|
H12
|
B:GOL502
|
3.4
|
56.1
|
1.0
|
H31
|
B:GOL502
|
3.7
|
58.9
|
1.0
|
HG22
|
B:THR231
|
3.8
|
32.9
|
1.0
|
C3
|
B:GOL502
|
3.8
|
49.0
|
1.0
|
NE2
|
B:HIS155
|
3.9
|
32.5
|
1.0
|
HE21
|
B:GLN71
|
3.9
|
32.4
|
1.0
|
NE2
|
B:GLN71
|
3.9
|
26.6
|
1.0
|
HG21
|
B:THR231
|
4.0
|
32.9
|
1.0
|
ND1
|
B:HIS211
|
4.1
|
31.0
|
1.0
|
CG
|
B:GLU143
|
4.1
|
29.4
|
1.0
|
CG
|
B:HIS211
|
4.2
|
29.8
|
1.0
|
CG
|
B:HIS232
|
4.2
|
27.5
|
1.0
|
H32
|
B:GOL502
|
4.3
|
58.9
|
1.0
|
ND1
|
B:HIS232
|
4.3
|
28.0
|
1.0
|
O
|
B:HOH692
|
4.3
|
33.2
|
1.0
|
HG3
|
B:GLU143
|
4.3
|
36.4
|
1.0
|
CG2
|
B:THR231
|
4.3
|
26.9
|
1.0
|
HG2
|
B:GLU143
|
4.3
|
36.4
|
1.0
|
O
|
B:HOH635
|
4.5
|
29.0
|
1.0
|
HD2
|
B:HIS155
|
4.5
|
39.0
|
1.0
|
CD2
|
B:HIS155
|
4.6
|
33.5
|
1.0
|
HG23
|
B:THR231
|
4.6
|
32.9
|
1.0
|
HB3
|
B:ALA236
|
4.8
|
29.5
|
1.0
|
O3
|
B:GOL502
|
4.8
|
52.3
|
1.0
|
CE1
|
B:HIS155
|
4.9
|
32.8
|
1.0
|
HD1
|
B:HIS211
|
4.9
|
38.4
|
1.0
|
OD1
|
B:ASP294
|
4.9
|
28.8
|
1.0
|
HE1
|
B:HIS155
|
5.0
|
37.8
|
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 07:58:21 2024
|