Magnesium in PDB 6b4j: Crystal Structure of Human GLE1 Ctd-NUP42 Gbm-DDX19B(Amppnp) Complex
Enzymatic activity of Crystal Structure of Human GLE1 Ctd-NUP42 Gbm-DDX19B(Amppnp) Complex
All present enzymatic activity of Crystal Structure of Human GLE1 Ctd-NUP42 Gbm-DDX19B(Amppnp) Complex:
3.6.4.13;
Protein crystallography data
The structure of Crystal Structure of Human GLE1 Ctd-NUP42 Gbm-DDX19B(Amppnp) Complex, PDB code: 6b4j
was solved by
D.H.Lin,
A.R.Correia,
S.W.Cai,
F.M.Huber,
C.A.Jette,
A.Hoelz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.43 /
3.40
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
87.940,
73.560,
145.860,
90.00,
95.07,
90.00
|
R / Rfree (%)
|
26.1 /
31.3
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Human GLE1 Ctd-NUP42 Gbm-DDX19B(Amppnp) Complex
(pdb code 6b4j). 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 Structure of Human GLE1 Ctd-NUP42 Gbm-DDX19B(Amppnp) Complex, PDB code: 6b4j:
Jump to Magnesium binding site number:
1;
2;
Magnesium binding site 1 out
of 2 in 6b4j
Go back to
Magnesium Binding Sites List in 6b4j
Magnesium binding site 1 out
of 2 in the Crystal Structure of Human GLE1 Ctd-NUP42 Gbm-DDX19B(Amppnp) Complex
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Crystal Structure of Human GLE1 Ctd-NUP42 Gbm-DDX19B(Amppnp) Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg503
b:86.1
occ:1.00
|
HZ3
|
E:LYS64
|
1.7
|
0.6
|
1.0
|
HZ1
|
E:LYS64
|
1.7
|
0.6
|
1.0
|
OG1
|
E:THR145
|
1.8
|
93.6
|
1.0
|
O2G
|
E:ANP504
|
2.0
|
0.8
|
1.0
|
NZ
|
E:LYS64
|
2.0
|
0.8
|
1.0
|
HOG2
|
E:ANP504
|
2.3
|
0.2
|
1.0
|
HZ2
|
E:LYS64
|
2.6
|
0.6
|
1.0
|
CB
|
E:THR145
|
3.0
|
0.4
|
1.0
|
HE2
|
E:LYS64
|
3.1
|
0.1
|
1.0
|
CE
|
E:LYS64
|
3.2
|
0.2
|
1.0
|
HB
|
E:THR145
|
3.3
|
0.5
|
1.0
|
PG
|
E:ANP504
|
3.3
|
0.5
|
1.0
|
OD2
|
E:ASP242
|
3.3
|
0.7
|
1.0
|
HG21
|
E:THR145
|
3.4
|
0.2
|
1.0
|
OE2
|
E:GLU243
|
3.6
|
0.2
|
1.0
|
N3B
|
E:ANP504
|
3.7
|
98.8
|
1.0
|
CG2
|
E:THR145
|
3.7
|
95.2
|
1.0
|
HE3
|
E:LYS64
|
3.8
|
0.1
|
1.0
|
O1B
|
E:ANP504
|
3.8
|
86.1
|
1.0
|
HG23
|
E:THR145
|
3.8
|
0.2
|
1.0
|
HNB1
|
E:ANP504
|
3.9
|
0.6
|
1.0
|
H
|
E:THR145
|
4.0
|
0.7
|
1.0
|
HOA2
|
E:ANP504
|
4.0
|
0.0
|
1.0
|
OD1
|
E:ASP242
|
4.1
|
0.5
|
1.0
|
O1G
|
E:ANP504
|
4.1
|
96.0
|
1.0
|
CG
|
E:ASP242
|
4.1
|
0.5
|
1.0
|
HD2
|
E:LYS64
|
4.2
|
0.6
|
1.0
|
CA
|
E:THR145
|
4.2
|
93.5
|
1.0
|
O2A
|
E:ANP504
|
4.2
|
84.2
|
1.0
|
HG3
|
E:GLU243
|
4.2
|
0.4
|
1.0
|
CD
|
E:LYS64
|
4.2
|
88.0
|
1.0
|
HA
|
E:THR145
|
4.3
|
0.2
|
1.0
|
HD3
|
E:LYS64
|
4.3
|
0.6
|
1.0
|
N
|
E:THR145
|
4.4
|
92.2
|
1.0
|
O3G
|
E:ANP504
|
4.4
|
0.9
|
1.0
|
PB
|
E:ANP504
|
4.5
|
87.6
|
1.0
|
HE2
|
E:PHE148
|
4.5
|
0.6
|
1.0
|
CD
|
E:GLU243
|
4.5
|
0.7
|
1.0
|
HG2
|
E:GLU243
|
4.6
|
0.4
|
1.0
|
HG22
|
E:THR145
|
4.6
|
0.2
|
1.0
|
CG
|
E:GLU243
|
4.7
|
0.9
|
1.0
|
OG1
|
E:THR178
|
4.7
|
91.0
|
1.0
|
HG1
|
E:THR178
|
4.8
|
0.1
|
1.0
|
O2B
|
E:ANP504
|
4.8
|
95.3
|
1.0
|
HB2
|
E:LYS144
|
4.8
|
0.3
|
1.0
|
HOG3
|
E:ANP504
|
4.9
|
0.7
|
1.0
|
PA
|
E:ANP504
|
5.0
|
84.5
|
1.0
|
|
Magnesium binding site 2 out
of 2 in 6b4j
Go back to
Magnesium Binding Sites List in 6b4j
Magnesium binding site 2 out
of 2 in the Crystal Structure of Human GLE1 Ctd-NUP42 Gbm-DDX19B(Amppnp) Complex
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Crystal Structure of Human GLE1 Ctd-NUP42 Gbm-DDX19B(Amppnp) Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg503
b:76.8
occ:1.00
|
HOG2
|
F:ANP504
|
1.7
|
0.2
|
1.0
|
OG1
|
F:THR145
|
1.9
|
83.0
|
1.0
|
O2G
|
F:ANP504
|
2.0
|
95.1
|
1.0
|
OD1
|
F:ASP242
|
2.9
|
1.0
|
1.0
|
HZ1
|
F:LYS64
|
2.9
|
0.6
|
1.0
|
HZ3
|
F:LYS64
|
3.2
|
0.6
|
1.0
|
CB
|
F:THR145
|
3.2
|
91.9
|
1.0
|
H
|
F:THR145
|
3.3
|
1.0
|
1.0
|
OD2
|
F:ASP242
|
3.3
|
0.3
|
1.0
|
HB2
|
F:LYS144
|
3.4
|
0.8
|
1.0
|
PG
|
F:ANP504
|
3.4
|
88.2
|
1.0
|
NZ
|
F:LYS64
|
3.5
|
0.7
|
1.0
|
CG
|
F:ASP242
|
3.5
|
0.7
|
1.0
|
O1B
|
F:ANP504
|
3.5
|
89.3
|
1.0
|
N
|
F:THR145
|
3.6
|
94.2
|
1.0
|
HE2
|
F:LYS144
|
3.6
|
0.6
|
1.0
|
HA
|
F:THR145
|
3.6
|
0.8
|
1.0
|
CA
|
F:THR145
|
3.7
|
95.7
|
1.0
|
HE2
|
F:PHE148
|
3.7
|
0.9
|
1.0
|
HB
|
F:THR145
|
3.8
|
0.2
|
1.0
|
O3G
|
F:ANP504
|
3.8
|
0.5
|
1.0
|
HG3
|
F:GLU243
|
3.8
|
0.5
|
1.0
|
HG2
|
F:GLU243
|
3.9
|
0.5
|
1.0
|
HOG3
|
F:ANP504
|
3.9
|
0.6
|
1.0
|
HZ2
|
F:LYS64
|
4.0
|
0.6
|
1.0
|
N3B
|
F:ANP504
|
4.0
|
81.2
|
1.0
|
HG23
|
F:THR145
|
4.1
|
0.1
|
1.0
|
O2B
|
F:ANP504
|
4.1
|
98.9
|
1.0
|
CG2
|
F:THR145
|
4.2
|
90.9
|
1.0
|
CB
|
F:LYS144
|
4.2
|
97.3
|
1.0
|
HB3
|
F:LYS144
|
4.2
|
0.8
|
1.0
|
CG
|
F:GLU243
|
4.3
|
0.8
|
1.0
|
OE2
|
F:GLU243
|
4.3
|
0.5
|
1.0
|
HG21
|
F:THR145
|
4.3
|
0.1
|
1.0
|
HE2
|
F:LYS64
|
4.4
|
0.2
|
1.0
|
PB
|
F:ANP504
|
4.4
|
83.1
|
1.0
|
C
|
F:LYS144
|
4.4
|
97.1
|
1.0
|
O1G
|
F:ANP504
|
4.5
|
94.1
|
1.0
|
CE
|
F:LYS64
|
4.6
|
0.7
|
1.0
|
CE
|
F:LYS144
|
4.6
|
0.0
|
1.0
|
CE2
|
F:PHE148
|
4.6
|
93.3
|
1.0
|
CD
|
F:GLU243
|
4.8
|
0.2
|
1.0
|
HZ1
|
F:LYS144
|
4.8
|
0.6
|
1.0
|
HNB1
|
F:ANP504
|
4.8
|
97.4
|
1.0
|
H
|
F:GLU243
|
4.8
|
0.8
|
1.0
|
HZ3
|
F:LYS144
|
4.8
|
0.6
|
1.0
|
O2A
|
F:ANP504
|
4.8
|
0.3
|
1.0
|
HOA2
|
F:ANP504
|
4.9
|
1.0
|
1.0
|
CA
|
F:LYS144
|
4.9
|
97.1
|
1.0
|
HOB2
|
F:ANP504
|
4.9
|
0.7
|
1.0
|
NZ
|
F:LYS144
|
5.0
|
0.7
|
1.0
|
CB
|
F:ASP242
|
5.0
|
0.0
|
1.0
|
|
Reference:
D.H.Lin,
A.R.Correia,
S.W.Cai,
F.M.Huber,
C.A.Jette,
A.Hoelz.
Structural and Functional Analysis of Mrna Export Regulation By the Nuclear Pore Complex. Nat Commun V. 9 2319 2018.
ISSN: ESSN 2041-1723
PubMed: 29899397
DOI: 10.1038/S41467-018-04459-3
Page generated: Mon Sep 30 19:30:35 2024
|