Magnesium in PDB 1z0a: Gdp-Bound RAB2A Gtpase
Protein crystallography data
The structure of Gdp-Bound RAB2A Gtpase, PDB code: 1z0a
was solved by
S.Eathiraj,
X.Pan,
C.Ritacco,
D.G.Lambright,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
10.00 /
2.12
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
98.773,
128.473,
68.236,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21.9 /
27.9
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Gdp-Bound RAB2A Gtpase
(pdb code 1z0a). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Gdp-Bound RAB2A Gtpase, PDB code: 1z0a:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 1z0a
Go back to
Magnesium Binding Sites List in 1z0a
Magnesium binding site 1 out
of 4 in the Gdp-Bound RAB2A Gtpase
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Gdp-Bound RAB2A Gtpase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1201
b:83.1
occ:1.00
|
OG
|
A:SER20
|
2.0
|
37.3
|
1.0
|
O2B
|
A:GDP1200
|
2.3
|
35.8
|
1.0
|
O
|
A:HOH1217
|
2.9
|
50.2
|
1.0
|
CB
|
A:ALA63
|
3.0
|
36.8
|
1.0
|
OD2
|
A:ASP61
|
3.0
|
41.7
|
1.0
|
CB
|
A:SER20
|
3.3
|
31.2
|
1.0
|
OD1
|
A:ASP61
|
3.5
|
35.1
|
1.0
|
PB
|
A:GDP1200
|
3.5
|
35.6
|
1.0
|
CG
|
A:ASP61
|
3.7
|
37.3
|
1.0
|
O3B
|
A:GDP1200
|
3.7
|
32.3
|
1.0
|
N
|
A:SER20
|
3.8
|
30.4
|
1.0
|
O
|
D:HOH4251
|
4.0
|
63.9
|
1.0
|
O
|
A:HOH1372
|
4.0
|
81.5
|
1.0
|
CD1
|
A:LEU37
|
4.0
|
71.5
|
1.0
|
O
|
A:HOH1357
|
4.0
|
66.5
|
1.0
|
CA
|
A:SER20
|
4.1
|
32.3
|
1.0
|
CA
|
A:ALA63
|
4.2
|
36.9
|
1.0
|
O1B
|
A:GDP1200
|
4.3
|
31.5
|
1.0
|
O2A
|
A:GDP1200
|
4.5
|
36.1
|
1.0
|
CE
|
A:LYS19
|
4.6
|
27.4
|
1.0
|
CB
|
A:LYS19
|
4.6
|
30.1
|
1.0
|
O3A
|
A:GDP1200
|
4.6
|
34.5
|
1.0
|
N
|
A:ALA63
|
4.6
|
34.7
|
1.0
|
CD2
|
A:LEU37
|
4.7
|
60.8
|
1.0
|
CG
|
A:LEU37
|
4.7
|
60.6
|
1.0
|
C
|
A:LYS19
|
4.8
|
30.3
|
1.0
|
PA
|
A:GDP1200
|
4.9
|
34.8
|
1.0
|
O1A
|
A:GDP1200
|
4.9
|
36.5
|
1.0
|
NZ
|
A:LYS19
|
5.0
|
27.5
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 1z0a
Go back to
Magnesium Binding Sites List in 1z0a
Magnesium binding site 2 out
of 4 in the Gdp-Bound RAB2A Gtpase
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Gdp-Bound RAB2A Gtpase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg2201
b:66.6
occ:1.00
|
O
|
B:HOH2209
|
2.0
|
44.8
|
1.0
|
OG
|
B:SER20
|
2.2
|
39.8
|
1.0
|
O
|
B:HOH2256
|
2.3
|
62.1
|
1.0
|
O
|
B:HOH2283
|
2.4
|
74.5
|
1.0
|
O2B
|
B:GDP2200
|
2.4
|
41.9
|
1.0
|
CB
|
B:SER20
|
3.5
|
35.0
|
1.0
|
PB
|
B:GDP2200
|
3.6
|
43.4
|
1.0
|
O3B
|
B:GDP2200
|
3.6
|
41.3
|
1.0
|
O
|
B:HOH2279
|
3.8
|
68.5
|
1.0
|
OD2
|
B:ASP61
|
3.9
|
46.1
|
1.0
|
O
|
B:HOH2276
|
4.2
|
57.5
|
1.0
|
N
|
B:SER20
|
4.2
|
33.3
|
1.0
|
O2A
|
B:GDP2200
|
4.4
|
43.0
|
1.0
|
OD1
|
B:ASP61
|
4.4
|
39.7
|
1.0
|
N
|
B:GLY64
|
4.4
|
55.1
|
1.0
|
O
|
B:THR62
|
4.5
|
42.0
|
1.0
|
CA
|
B:SER20
|
4.5
|
34.3
|
1.0
|
O1B
|
B:GDP2200
|
4.5
|
41.8
|
1.0
|
O
|
B:HOH2266
|
4.5
|
77.1
|
1.0
|
CA
|
B:ALA63
|
4.6
|
48.8
|
1.0
|
CG
|
B:ASP61
|
4.6
|
37.8
|
1.0
|
O3A
|
B:GDP2200
|
4.7
|
40.6
|
1.0
|
OD1
|
B:ASP36
|
4.8
|
64.6
|
1.0
|
PA
|
B:GDP2200
|
4.9
|
38.3
|
1.0
|
CE
|
B:LYS19
|
4.9
|
33.6
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 1z0a
Go back to
Magnesium Binding Sites List in 1z0a
Magnesium binding site 3 out
of 4 in the Gdp-Bound RAB2A Gtpase
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Gdp-Bound RAB2A Gtpase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg3201
b:51.3
occ:1.00
|
O2B
|
C:GDP3200
|
2.4
|
30.2
|
1.0
|
OD2
|
C:ASP61
|
2.7
|
35.3
|
1.0
|
CB
|
C:ALA63
|
3.0
|
34.1
|
1.0
|
O
|
C:HOH3227
|
3.1
|
41.7
|
1.0
|
OD1
|
C:ASP61
|
3.2
|
35.3
|
1.0
|
CG
|
C:ASP61
|
3.3
|
29.8
|
1.0
|
PB
|
C:GDP3200
|
3.5
|
33.6
|
1.0
|
O3B
|
C:GDP3200
|
3.5
|
26.5
|
1.0
|
CD2
|
C:LEU37
|
3.8
|
52.8
|
1.0
|
CE
|
C:LYS19
|
3.8
|
26.4
|
1.0
|
NZ
|
C:LYS19
|
4.0
|
22.8
|
1.0
|
CB
|
C:SER20
|
4.0
|
32.2
|
1.0
|
O1B
|
C:GDP3200
|
4.0
|
29.8
|
1.0
|
CD1
|
C:LEU37
|
4.0
|
53.8
|
1.0
|
N
|
C:SER20
|
4.1
|
28.0
|
1.0
|
CB
|
C:LYS19
|
4.1
|
25.8
|
1.0
|
CA
|
C:ALA63
|
4.4
|
36.6
|
1.0
|
OE2
|
C:GLU66
|
4.5
|
42.2
|
1.0
|
CG
|
C:LEU37
|
4.5
|
50.2
|
1.0
|
CA
|
C:SER20
|
4.5
|
29.0
|
1.0
|
O
|
C:HOH3377
|
4.6
|
76.5
|
1.0
|
N
|
C:ALA63
|
4.7
|
33.2
|
1.0
|
CB
|
C:ASP61
|
4.8
|
27.0
|
1.0
|
C
|
C:LYS19
|
4.8
|
26.9
|
1.0
|
O3A
|
C:GDP3200
|
4.9
|
30.7
|
1.0
|
CD
|
C:LYS19
|
4.9
|
19.9
|
1.0
|
CG
|
C:LYS19
|
4.9
|
22.0
|
1.0
|
CA
|
C:LYS19
|
5.0
|
24.0
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 1z0a
Go back to
Magnesium Binding Sites List in 1z0a
Magnesium binding site 4 out
of 4 in the Gdp-Bound RAB2A Gtpase
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Gdp-Bound RAB2A Gtpase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg4201
b:83.1
occ:1.00
|
O2B
|
D:GDP4200
|
2.1
|
35.8
|
1.0
|
O
|
D:HOH4292
|
2.1
|
80.5
|
1.0
|
PB
|
D:GDP4200
|
3.3
|
35.6
|
1.0
|
CB
|
D:SER20
|
3.4
|
48.6
|
1.0
|
O3B
|
D:GDP4200
|
3.5
|
32.3
|
1.0
|
OD2
|
D:ASP61
|
3.7
|
42.1
|
1.0
|
O2A
|
D:GDP4200
|
4.1
|
36.1
|
1.0
|
O
|
D:HOH4230
|
4.1
|
60.3
|
1.0
|
OG
|
D:SER20
|
4.2
|
54.9
|
1.0
|
N
|
D:SER20
|
4.2
|
46.3
|
1.0
|
O1B
|
D:GDP4200
|
4.2
|
31.5
|
1.0
|
CA
|
D:SER20
|
4.3
|
48.2
|
1.0
|
O3A
|
D:GDP4200
|
4.4
|
34.5
|
1.0
|
CG
|
D:ASP61
|
4.6
|
41.6
|
1.0
|
OD1
|
D:ASP61
|
4.6
|
42.0
|
1.0
|
PA
|
D:GDP4200
|
4.7
|
34.8
|
1.0
|
CA
|
D:ALA63
|
4.7
|
53.1
|
1.0
|
O1A
|
D:GDP4200
|
4.9
|
36.5
|
1.0
|
O
|
D:THR62
|
5.0
|
46.9
|
1.0
|
|
Reference:
S.Eathiraj,
X.Pan,
C.Ritacco,
D.G.Lambright.
Structural Basis of Family-Wide Rab Gtpase Recognition By Rabenosyn-5. Nature V. 436 415 2005.
ISSN: ISSN 0028-0836
PubMed: 16034420
DOI: 10.1038/NATURE03798
Page generated: Tue Aug 13 19:59:16 2024
|