Sodium in PDB 4osx: Structure of Uncleaved Glycine-Bound Human L-Asparaginase Protein
Enzymatic activity of Structure of Uncleaved Glycine-Bound Human L-Asparaginase Protein
All present enzymatic activity of Structure of Uncleaved Glycine-Bound Human L-Asparaginase Protein:
3.4.19.5;
3.5.1.1;
Protein crystallography data
The structure of Structure of Uncleaved Glycine-Bound Human L-Asparaginase Protein, PDB code: 4osx
was solved by
J.Nomme,
A.Lavie,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.39 /
1.95
|
Space group
|
P 65
|
Cell size a, b, c (Å), α, β, γ (°)
|
59.940,
59.940,
301.100,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
16.7 /
20.9
|
Sodium Binding Sites:
The binding sites of Sodium atom in the Structure of Uncleaved Glycine-Bound Human L-Asparaginase Protein
(pdb code 4osx). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the
Structure of Uncleaved Glycine-Bound Human L-Asparaginase Protein, PDB code: 4osx:
Jump to Sodium binding site number:
1;
2;
Sodium binding site 1 out
of 2 in 4osx
Go back to
Sodium Binding Sites List in 4osx
Sodium binding site 1 out
of 2 in the Structure of Uncleaved Glycine-Bound Human L-Asparaginase Protein
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Structure of Uncleaved Glycine-Bound Human L-Asparaginase Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na401
b:22.9
occ:1.00
|
O
|
A:CYS65
|
2.2
|
24.8
|
1.0
|
O
|
A:ASP58
|
2.3
|
20.5
|
1.0
|
O
|
A:ALA63
|
2.4
|
20.3
|
1.0
|
O
|
A:GLU56
|
2.6
|
20.9
|
1.0
|
O
|
A:PHE61
|
2.6
|
21.3
|
1.0
|
O
|
A:LEU55
|
3.0
|
20.1
|
1.0
|
C
|
A:ASP58
|
3.2
|
21.0
|
1.0
|
C
|
A:GLU56
|
3.4
|
20.6
|
1.0
|
C
|
A:CYS65
|
3.4
|
24.7
|
1.0
|
C
|
A:ALA63
|
3.6
|
20.5
|
1.0
|
C
|
A:PHE61
|
3.6
|
21.3
|
1.0
|
CA
|
A:GLU56
|
3.9
|
20.9
|
1.0
|
N
|
A:PHE61
|
3.9
|
21.8
|
1.0
|
N
|
A:ASP58
|
3.9
|
20.3
|
1.0
|
N
|
A:CYS65
|
4.0
|
23.6
|
1.0
|
CA
|
A:PHE61
|
4.0
|
21.2
|
1.0
|
N
|
A:ALA63
|
4.0
|
20.0
|
1.0
|
N
|
A:PRO59
|
4.0
|
21.5
|
1.0
|
C
|
A:LEU55
|
4.1
|
20.5
|
1.0
|
CA
|
A:PRO59
|
4.1
|
22.1
|
1.0
|
CA
|
A:ASP58
|
4.1
|
20.4
|
1.0
|
CB
|
A:PHE61
|
4.1
|
21.1
|
1.0
|
CA
|
A:CYS65
|
4.2
|
24.7
|
1.0
|
C
|
A:ASP57
|
4.2
|
20.4
|
1.0
|
N
|
A:ASP57
|
4.3
|
20.6
|
1.0
|
C
|
A:PRO59
|
4.3
|
22.1
|
1.0
|
N
|
A:GLY66
|
4.3
|
25.0
|
1.0
|
CA
|
A:ALA63
|
4.4
|
20.2
|
1.0
|
C
|
A:GLY64
|
4.4
|
22.7
|
1.0
|
CA
|
A:GLY66
|
4.5
|
25.1
|
1.0
|
N
|
A:GLU56
|
4.5
|
20.3
|
1.0
|
O
|
A:PRO59
|
4.5
|
21.8
|
1.0
|
O
|
A:ASP57
|
4.5
|
20.7
|
1.0
|
N
|
A:GLY64
|
4.6
|
20.7
|
1.0
|
CB
|
A:CYS65
|
4.6
|
25.3
|
1.0
|
CA
|
A:ASP57
|
4.7
|
20.5
|
1.0
|
CB
|
A:ASP58
|
4.7
|
20.3
|
1.0
|
N
|
A:GLU60
|
4.7
|
22.1
|
1.0
|
CA
|
A:GLY64
|
4.8
|
21.8
|
1.0
|
N
|
A:ASN62
|
4.8
|
21.1
|
1.0
|
C
|
A:GLY66
|
4.9
|
25.0
|
1.0
|
O
|
A:GLY64
|
4.9
|
22.1
|
1.0
|
CB
|
A:ALA63
|
4.9
|
20.0
|
1.0
|
|
Sodium binding site 2 out
of 2 in 4osx
Go back to
Sodium Binding Sites List in 4osx
Sodium binding site 2 out
of 2 in the Structure of Uncleaved Glycine-Bound Human L-Asparaginase Protein
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Structure of Uncleaved Glycine-Bound Human L-Asparaginase Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na401
b:19.0
occ:1.00
|
O
|
B:ASP58
|
2.2
|
26.4
|
1.0
|
O
|
B:ALA63
|
2.4
|
22.8
|
1.0
|
O
|
B:CYS65
|
2.4
|
24.9
|
1.0
|
O
|
B:LEU55
|
2.4
|
23.3
|
1.0
|
O
|
B:GLU56
|
2.8
|
24.9
|
1.0
|
O
|
B:PHE61
|
2.9
|
24.1
|
1.0
|
C
|
B:ASP58
|
3.2
|
26.3
|
1.0
|
C
|
B:GLU56
|
3.4
|
24.9
|
1.0
|
C
|
B:CYS65
|
3.5
|
24.5
|
1.0
|
C
|
B:LEU55
|
3.5
|
23.2
|
1.0
|
C
|
B:ALA63
|
3.5
|
22.3
|
1.0
|
CA
|
B:GLU56
|
3.6
|
24.2
|
1.0
|
C
|
B:PHE61
|
3.7
|
24.3
|
1.0
|
N
|
B:ASP58
|
3.8
|
25.7
|
1.0
|
N
|
B:GLU56
|
4.0
|
23.2
|
1.0
|
N
|
B:ALA63
|
4.0
|
21.9
|
1.0
|
CA
|
B:ASP58
|
4.0
|
25.9
|
1.0
|
N
|
B:CYS65
|
4.1
|
24.2
|
1.0
|
CB
|
B:PHE61
|
4.1
|
25.1
|
1.0
|
C
|
B:GLY64
|
4.1
|
23.8
|
1.0
|
N
|
B:PHE61
|
4.2
|
25.3
|
1.0
|
CA
|
B:PHE61
|
4.2
|
25.1
|
1.0
|
N
|
B:PRO59
|
4.2
|
26.2
|
1.0
|
CA
|
B:CYS65
|
4.3
|
24.5
|
1.0
|
CA
|
B:PRO59
|
4.3
|
26.6
|
1.0
|
N
|
B:GLY66
|
4.3
|
24.5
|
1.0
|
CA
|
B:ALA63
|
4.3
|
22.3
|
1.0
|
O
|
B:GLY64
|
4.4
|
23.0
|
1.0
|
N
|
B:ASP57
|
4.4
|
25.4
|
1.0
|
CA
|
B:GLY66
|
4.4
|
24.7
|
1.0
|
C
|
B:ASP57
|
4.5
|
25.7
|
1.0
|
N
|
B:GLY64
|
4.5
|
22.7
|
1.0
|
CB
|
B:ASP58
|
4.6
|
26.2
|
1.0
|
CA
|
B:GLY64
|
4.6
|
22.9
|
1.0
|
CB
|
B:ALA63
|
4.7
|
21.8
|
1.0
|
N
|
B:ASN62
|
4.7
|
23.6
|
1.0
|
C
|
B:PRO59
|
4.7
|
26.6
|
1.0
|
CB
|
B:CYS65
|
4.8
|
24.7
|
1.0
|
CA
|
B:LEU55
|
4.8
|
23.1
|
1.0
|
C
|
B:GLY66
|
4.9
|
24.6
|
1.0
|
N
|
B:GLU60
|
4.9
|
26.6
|
1.0
|
CB
|
B:GLU56
|
5.0
|
24.1
|
1.0
|
CA
|
B:ASP57
|
5.0
|
25.6
|
1.0
|
C
|
B:ASN62
|
5.0
|
22.6
|
1.0
|
|
Reference:
Y.Su,
C.S.Karamitros,
J.Nomme,
T.Mcsorley,
M.Konrad,
A.Lavie.
Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase. Chem.Biol. V. 20 533 2013.
ISSN: ISSN 1074-5521
PubMed: 23601642
DOI: 10.1016/J.CHEMBIOL.2013.03.006
Page generated: Mon Oct 7 17:32:17 2024
|