Magnesium in PDB 7wua: Crystal Structures of FADD32 From Corynebacterium Diphtheriae
Protein crystallography data
The structure of Crystal Structures of FADD32 From Corynebacterium Diphtheriae, PDB code: 7wua
was solved by
X.Liu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.10 /
2.00
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
108.647,
97.535,
142.043,
90,
95.93,
90
|
R / Rfree (%)
|
18.5 /
22.4
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structures of FADD32 From Corynebacterium Diphtheriae
(pdb code 7wua). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the
Crystal Structures of FADD32 From Corynebacterium Diphtheriae, PDB code: 7wua:
Jump to Magnesium binding site number:
1;
2;
Magnesium binding site 1 out
of 2 in 7wua
Go back to
Magnesium Binding Sites List in 7wua
Magnesium binding site 1 out
of 2 in the Crystal Structures of FADD32 From Corynebacterium Diphtheriae
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Crystal Structures of FADD32 From Corynebacterium Diphtheriae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg703
b:30.0
occ:1.00
|
O
|
A:HOH924
|
1.8
|
23.6
|
1.0
|
O
|
A:HOH956
|
2.0
|
24.0
|
1.0
|
O
|
A:HOH1001
|
2.0
|
18.6
|
1.0
|
O3G
|
A:ANP701
|
2.2
|
28.1
|
1.0
|
O1B
|
A:ANP701
|
2.3
|
21.1
|
1.0
|
O
|
A:HOH895
|
2.4
|
20.0
|
1.0
|
PG
|
A:ANP701
|
3.3
|
31.5
|
1.0
|
O
|
A:HOH1135
|
3.4
|
34.1
|
1.0
|
O2G
|
A:ANP701
|
3.5
|
30.8
|
1.0
|
PB
|
A:ANP701
|
3.5
|
27.7
|
1.0
|
O
|
A:HOH849
|
3.7
|
26.9
|
1.0
|
O
|
A:HOH1185
|
3.8
|
32.9
|
1.0
|
N3B
|
A:ANP701
|
3.9
|
24.6
|
1.0
|
OE2
|
A:GLU356
|
4.1
|
18.6
|
1.0
|
NH1
|
A:ARG492
|
4.2
|
23.9
|
1.0
|
O3A
|
A:ANP701
|
4.2
|
29.3
|
1.0
|
O
|
A:HOH1192
|
4.2
|
23.7
|
1.0
|
HO3'
|
A:ANP701
|
4.2
|
16.6
|
1.0
|
O
|
A:HOH1010
|
4.3
|
20.3
|
1.0
|
H5'1
|
A:ANP701
|
4.3
|
21.1
|
1.0
|
OE1
|
A:GLU356
|
4.4
|
13.6
|
1.0
|
H4'
|
A:ANP701
|
4.4
|
22.3
|
1.0
|
O1G
|
A:ANP701
|
4.5
|
32.4
|
1.0
|
CD
|
A:GLU356
|
4.6
|
21.6
|
1.0
|
O3'
|
A:ANP701
|
4.7
|
13.9
|
1.0
|
O2B
|
A:ANP701
|
4.7
|
21.7
|
1.0
|
O2A
|
A:ANP701
|
4.7
|
16.3
|
1.0
|
HNB1
|
A:ANP701
|
4.8
|
29.5
|
1.0
|
PA
|
A:ANP701
|
4.9
|
24.6
|
1.0
|
|
Magnesium binding site 2 out
of 2 in 7wua
Go back to
Magnesium Binding Sites List in 7wua
Magnesium binding site 2 out
of 2 in the Crystal Structures of FADD32 From Corynebacterium Diphtheriae
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Crystal Structures of FADD32 From Corynebacterium Diphtheriae within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg703
b:30.0
occ:1.00
|
O
|
B:HOH1035
|
2.0
|
28.4
|
1.0
|
O
|
B:HOH961
|
2.2
|
20.5
|
1.0
|
O
|
B:HOH929
|
2.5
|
22.3
|
1.0
|
O1B
|
B:ANP701
|
2.6
|
66.3
|
1.0
|
O3G
|
B:ANP701
|
2.6
|
28.1
|
1.0
|
O
|
B:HOH865
|
2.6
|
25.3
|
1.0
|
O1G
|
B:ANP701
|
3.2
|
51.2
|
1.0
|
PG
|
B:ANP701
|
3.3
|
40.1
|
1.0
|
PB
|
B:ANP701
|
3.4
|
45.2
|
1.0
|
N3B
|
B:ANP701
|
3.6
|
39.2
|
1.0
|
NH1
|
B:ARG492
|
3.7
|
27.1
|
1.0
|
O3A
|
B:ANP701
|
3.9
|
44.8
|
1.0
|
H4'
|
B:ANP701
|
4.1
|
24.4
|
1.0
|
H5'1
|
B:ANP701
|
4.3
|
22.2
|
1.0
|
O
|
B:HOH1121
|
4.3
|
30.9
|
1.0
|
HNB1
|
B:ANP701
|
4.4
|
47.0
|
1.0
|
O2B
|
B:ANP701
|
4.4
|
43.0
|
1.0
|
O
|
B:HOH946
|
4.5
|
20.1
|
1.0
|
HO3'
|
B:ANP701
|
4.5
|
21.6
|
1.0
|
OE2
|
B:GLU356
|
4.5
|
15.7
|
1.0
|
O2A
|
B:ANP701
|
4.6
|
24.0
|
1.0
|
O2G
|
B:ANP701
|
4.6
|
48.7
|
1.0
|
O3'
|
B:ANP701
|
4.6
|
18.0
|
1.0
|
OE1
|
B:GLU356
|
4.7
|
15.4
|
1.0
|
PA
|
B:ANP701
|
4.7
|
25.2
|
1.0
|
CZ
|
B:ARG492
|
4.8
|
35.5
|
1.0
|
C4'
|
B:ANP701
|
4.8
|
20.4
|
1.0
|
C5'
|
B:ANP701
|
4.9
|
18.5
|
1.0
|
O5'
|
B:ANP701
|
5.0
|
20.2
|
1.0
|
NH1
|
B:ARG594
|
5.0
|
28.6
|
1.0
|
|
Reference:
R.Chen,
J.Yuan,
X.Shi,
W.Tang.
Crystal Structures of FADD32 and PKS13-Acp Domain From Corynebacterium Diphtheriae Biochem Biophys Res Commun V. 590 152 2022.
ISSN: ISSN 0006-291X
Page generated: Thu Oct 3 11:21:59 2024
|