Magnesium in PDB 3tgp: Room Temperature H-Ras
Protein crystallography data
The structure of Room Temperature H-Ras, PDB code: 3tgp
was solved by
J.S.Fraser,
T.Alber,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
31.88 /
1.31
|
Space group
|
P 32 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
40.100,
40.100,
160.600,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
16.6 /
21.3
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Room Temperature H-Ras
(pdb code 3tgp). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the
Room Temperature H-Ras, PDB code: 3tgp:
Magnesium binding site 1 out
of 1 in 3tgp
Go back to
Magnesium Binding Sites List in 3tgp
Magnesium binding site 1 out
of 1 in the Room Temperature H-Ras
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Room Temperature H-Ras within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg168
b:15.2
occ:1.00
|
HG1
|
A:THR35
|
1.9
|
16.5
|
0.3
|
HG
|
A:SER17
|
1.9
|
22.1
|
0.8
|
HG
|
A:SER17
|
1.9
|
16.6
|
0.2
|
HG1
|
A:THR35
|
1.9
|
19.0
|
0.7
|
O3G
|
A:GNP167
|
2.0
|
15.8
|
1.0
|
O2B
|
A:GNP167
|
2.0
|
13.2
|
1.0
|
OG
|
A:SER17
|
2.1
|
13.8
|
0.2
|
OG
|
A:SER17
|
2.1
|
18.4
|
0.8
|
O
|
A:HOH170
|
2.1
|
16.5
|
1.0
|
O
|
A:HOH171
|
2.1
|
14.4
|
1.0
|
OG1
|
A:THR35
|
2.1
|
13.8
|
0.3
|
OG1
|
A:THR35
|
2.2
|
15.9
|
0.7
|
HB
|
A:THR35
|
2.9
|
20.1
|
0.7
|
HB
|
A:THR35
|
3.0
|
18.7
|
0.3
|
CB
|
A:THR35
|
3.1
|
16.8
|
0.7
|
HB2
|
A:SER17
|
3.1
|
22.1
|
0.8
|
CB
|
A:THR35
|
3.1
|
15.6
|
0.3
|
CB
|
A:SER17
|
3.1
|
18.4
|
0.8
|
HB2
|
A:SER17
|
3.2
|
16.5
|
0.2
|
PB
|
A:GNP167
|
3.2
|
13.8
|
1.0
|
CB
|
A:SER17
|
3.2
|
13.7
|
0.2
|
PG
|
A:GNP167
|
3.2
|
15.1
|
1.0
|
H
|
A:SER17
|
3.2
|
15.0
|
1.0
|
N3B
|
A:GNP167
|
3.3
|
13.4
|
1.0
|
H
|
A:THR35
|
3.5
|
21.0
|
1.0
|
OD2
|
A:ASP57
|
3.8
|
21.4
|
0.5
|
HB3
|
A:SER17
|
3.8
|
22.1
|
0.8
|
HB3
|
A:SER17
|
3.8
|
16.5
|
0.2
|
N
|
A:SER17
|
3.9
|
12.5
|
1.0
|
HB2
|
A:LYS16
|
3.9
|
14.2
|
1.0
|
N
|
A:THR35
|
3.9
|
17.5
|
1.0
|
HG21
|
A:THR35
|
4.0
|
25.0
|
0.7
|
OD2
|
A:ASP57
|
4.0
|
10.6
|
0.5
|
HG21
|
A:THR35
|
4.1
|
23.7
|
0.3
|
CA
|
A:SER17
|
4.1
|
11.9
|
1.0
|
O2G
|
A:GNP167
|
4.1
|
15.0
|
1.0
|
HE2
|
A:LYS16
|
4.1
|
18.9
|
1.0
|
OD1
|
A:ASP57
|
4.1
|
15.6
|
0.5
|
CA
|
A:THR35
|
4.1
|
15.5
|
1.0
|
O2A
|
A:GNP167
|
4.1
|
15.0
|
1.0
|
O1B
|
A:GNP167
|
4.2
|
15.9
|
1.0
|
CG2
|
A:THR35
|
4.2
|
20.9
|
0.7
|
CG2
|
A:THR35
|
4.2
|
19.7
|
0.3
|
O3A
|
A:GNP167
|
4.2
|
13.9
|
1.0
|
O
|
A:THR58
|
4.2
|
16.8
|
0.5
|
O1G
|
A:GNP167
|
4.3
|
17.3
|
1.0
|
O
|
A:HOH178
|
4.3
|
23.8
|
1.0
|
O
|
A:ASP33
|
4.4
|
16.9
|
0.3
|
HA
|
A:SER17
|
4.4
|
14.3
|
1.0
|
OD1
|
A:ASP57
|
4.4
|
20.4
|
0.5
|
CG
|
A:ASP57
|
4.4
|
8.5
|
0.5
|
O
|
A:ASP33
|
4.5
|
12.7
|
0.5
|
PA
|
A:GNP167
|
4.5
|
14.5
|
1.0
|
CG
|
A:ASP57
|
4.5
|
21.1
|
0.5
|
HA
|
A:PRO34
|
4.5
|
20.2
|
1.0
|
O1A
|
A:GNP167
|
4.6
|
15.4
|
1.0
|
HA
|
A:THR35
|
4.6
|
18.6
|
1.0
|
HG23
|
A:THR35
|
4.6
|
23.7
|
0.3
|
HG23
|
A:THR35
|
4.7
|
25.0
|
0.7
|
O
|
A:THR58
|
4.7
|
13.1
|
0.5
|
O
|
A:ASP33
|
4.7
|
18.8
|
0.2
|
HZ1
|
A:LYS16
|
4.8
|
17.1
|
1.0
|
CB
|
A:LYS16
|
4.8
|
11.8
|
1.0
|
C
|
A:PRO34
|
4.8
|
17.6
|
1.0
|
HG22
|
A:THR35
|
4.9
|
25.0
|
0.7
|
HZ3
|
A:LYS16
|
4.9
|
17.1
|
1.0
|
HG22
|
A:THR35
|
4.9
|
23.7
|
0.3
|
C
|
A:LYS16
|
4.9
|
12.4
|
1.0
|
CE
|
A:LYS16
|
5.0
|
15.7
|
1.0
|
HA
|
A:ALA59
|
5.0
|
19.8
|
1.0
|
|
Reference:
J.S.Fraser,
H.Van Den Bedem,
A.J.Samelson,
P.T.Lang,
J.M.Holton,
N.Echols,
T.Alber.
Accessing Protein Conformational Ensembles Using Room-Temperature X-Ray Crystallography. Proc.Natl.Acad.Sci.Usa V. 108 16247 2011.
ISSN: ISSN 0027-8424
PubMed: 21918110
DOI: 10.1073/PNAS.1111325108
Page generated: Thu Aug 15 12:06:23 2024
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