Sodium in PDB 4pvp: Crystal Structure of Malonate-Bound Human L-Asparaginase Protein
Enzymatic activity of Crystal Structure of Malonate-Bound Human L-Asparaginase Protein
All present enzymatic activity of Crystal Structure of Malonate-Bound Human L-Asparaginase Protein:
3.4.19.5;
3.5.1.1;
Protein crystallography data
The structure of Crystal Structure of Malonate-Bound Human L-Asparaginase Protein, PDB code: 4pvp
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)
|
29.73 /
1.85
|
Space group
|
P 65
|
Cell size a, b, c (Å), α, β, γ (°)
|
59.459,
59.459,
298.900,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
16.1 /
20.4
|
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Malonate-Bound Human L-Asparaginase Protein
(pdb code 4pvp). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the
Crystal Structure of Malonate-Bound Human L-Asparaginase Protein, PDB code: 4pvp:
Jump to Sodium binding site number:
1;
2;
Sodium binding site 1 out
of 2 in 4pvp
Go back to
Sodium Binding Sites List in 4pvp
Sodium binding site 1 out
of 2 in the Crystal Structure of Malonate-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 Crystal Structure of Malonate-Bound Human L-Asparaginase Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na402
b:23.5
occ:1.00
|
O
|
A:ALA63
|
2.3
|
21.4
|
1.0
|
O
|
A:ASP58
|
2.4
|
23.9
|
1.0
|
O
|
A:CYS65
|
2.4
|
22.4
|
1.0
|
O
|
A:GLU56
|
2.5
|
20.6
|
1.0
|
O
|
A:LEU55
|
2.7
|
20.2
|
1.0
|
O
|
A:PHE61
|
2.8
|
22.6
|
1.0
|
C
|
A:GLU56
|
3.2
|
20.8
|
1.0
|
C
|
A:ASP58
|
3.3
|
24.0
|
1.0
|
C
|
A:ALA63
|
3.5
|
21.0
|
1.0
|
C
|
A:CYS65
|
3.5
|
22.3
|
1.0
|
CA
|
A:GLU56
|
3.6
|
20.1
|
1.0
|
C
|
A:PHE61
|
3.6
|
22.2
|
1.0
|
C
|
A:LEU55
|
3.7
|
20.4
|
1.0
|
N
|
A:ASP58
|
3.9
|
23.2
|
1.0
|
N
|
A:PHE61
|
3.9
|
23.1
|
1.0
|
CB
|
A:PHE61
|
4.0
|
22.3
|
1.0
|
N
|
A:ALA63
|
4.0
|
21.1
|
1.0
|
N
|
A:CYS65
|
4.0
|
22.2
|
1.0
|
CA
|
A:PHE61
|
4.0
|
22.7
|
1.0
|
N
|
A:PRO59
|
4.1
|
24.1
|
1.0
|
N
|
A:GLU56
|
4.1
|
20.1
|
1.0
|
CA
|
A:ASP58
|
4.2
|
23.7
|
1.0
|
CA
|
A:PRO59
|
4.2
|
24.6
|
1.0
|
C
|
A:GLY64
|
4.2
|
21.6
|
1.0
|
N
|
A:ASP57
|
4.3
|
21.2
|
1.0
|
CA
|
A:CYS65
|
4.3
|
22.5
|
1.0
|
CA
|
A:ALA63
|
4.4
|
21.0
|
1.0
|
C
|
A:ASP57
|
4.4
|
23.1
|
1.0
|
N
|
A:GLY66
|
4.4
|
22.6
|
1.0
|
N
|
A:GLY64
|
4.5
|
21.0
|
1.0
|
C
|
A:PRO59
|
4.5
|
24.6
|
1.0
|
CA
|
A:GLY66
|
4.5
|
22.6
|
1.0
|
CA
|
A:GLY64
|
4.6
|
21.2
|
1.0
|
O
|
A:GLY64
|
4.6
|
21.6
|
1.0
|
N
|
A:ASN62
|
4.7
|
21.8
|
1.0
|
CB
|
A:ASP58
|
4.7
|
23.7
|
1.0
|
N
|
A:GLU60
|
4.8
|
24.5
|
1.0
|
CA
|
A:ASP57
|
4.8
|
22.2
|
1.0
|
CB
|
A:CYS65
|
4.8
|
22.9
|
1.0
|
C
|
A:GLY66
|
4.8
|
22.8
|
1.0
|
CB
|
A:ALA63
|
4.8
|
20.5
|
1.0
|
O
|
A:ASP57
|
4.9
|
23.4
|
1.0
|
CB
|
A:GLU56
|
5.0
|
19.9
|
1.0
|
O
|
A:PRO59
|
5.0
|
24.9
|
1.0
|
|
Sodium binding site 2 out
of 2 in 4pvp
Go back to
Sodium Binding Sites List in 4pvp
Sodium binding site 2 out
of 2 in the Crystal Structure of Malonate-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 Crystal Structure of Malonate-Bound Human L-Asparaginase Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na401
b:27.1
occ:1.00
|
O
|
B:CYS65
|
2.2
|
22.2
|
1.0
|
O
|
B:ASP58
|
2.4
|
21.1
|
1.0
|
O
|
B:ALA63
|
2.4
|
18.7
|
1.0
|
O
|
B:LEU55
|
2.5
|
19.2
|
1.0
|
O
|
B:PHE61
|
2.6
|
18.5
|
1.0
|
O
|
B:GLU56
|
2.8
|
19.6
|
1.0
|
C
|
B:CYS65
|
3.3
|
22.4
|
1.0
|
C
|
B:GLU56
|
3.3
|
19.6
|
1.0
|
C
|
B:ASP58
|
3.3
|
21.4
|
1.0
|
C
|
B:ALA63
|
3.6
|
18.5
|
1.0
|
C
|
B:LEU55
|
3.6
|
19.5
|
1.0
|
CA
|
B:GLU56
|
3.6
|
19.2
|
1.0
|
C
|
B:PHE61
|
3.6
|
18.8
|
1.0
|
N
|
B:CYS65
|
3.9
|
21.8
|
1.0
|
N
|
B:ASP58
|
4.0
|
21.0
|
1.0
|
N
|
B:ALA63
|
4.0
|
17.8
|
1.0
|
N
|
B:GLU56
|
4.1
|
19.4
|
1.0
|
N
|
B:PHE61
|
4.1
|
20.1
|
1.0
|
CA
|
B:CYS65
|
4.1
|
22.4
|
1.0
|
CA
|
B:PHE61
|
4.2
|
19.6
|
1.0
|
CB
|
B:PHE61
|
4.2
|
19.8
|
1.0
|
CA
|
B:ASP58
|
4.2
|
21.4
|
1.0
|
N
|
B:PRO59
|
4.2
|
21.6
|
1.0
|
N
|
B:GLY66
|
4.3
|
22.5
|
1.0
|
N
|
B:ASP57
|
4.3
|
19.9
|
1.0
|
CA
|
B:PRO59
|
4.3
|
21.8
|
1.0
|
C
|
B:ASP57
|
4.4
|
21.1
|
1.0
|
C
|
B:GLY64
|
4.4
|
20.9
|
1.0
|
CA
|
B:ALA63
|
4.4
|
18.3
|
1.0
|
CA
|
B:GLY66
|
4.5
|
23.1
|
1.0
|
N
|
B:GLY64
|
4.5
|
18.5
|
1.0
|
C
|
B:PRO59
|
4.6
|
22.1
|
1.0
|
CB
|
B:CYS65
|
4.6
|
22.7
|
1.0
|
CA
|
B:GLY64
|
4.7
|
20.2
|
1.0
|
CB
|
B:ALA63
|
4.8
|
17.6
|
1.0
|
O
|
B:ASP57
|
4.8
|
21.5
|
1.0
|
N
|
B:ASN62
|
4.8
|
17.9
|
1.0
|
CB
|
B:ASP58
|
4.8
|
21.9
|
1.0
|
C
|
B:GLY66
|
4.9
|
23.2
|
1.0
|
CA
|
B:ASP57
|
4.9
|
20.8
|
1.0
|
CA
|
B:LEU55
|
4.9
|
19.7
|
1.0
|
N
|
B:GLU60
|
4.9
|
22.0
|
1.0
|
O
|
B:PRO59
|
5.0
|
22.5
|
1.0
|
|
Reference:
J.Nomme,
Y.Su,
M.Konrad,
A.Lavie.
Structures of Apo and Product-Bound Human L-Asparaginase: Insights Into the Mechanism of Autoproteolysis and Substrate Hydrolysis. Biochemistry V. 51 6816 2012.
ISSN: ISSN 0006-2960
PubMed: 22861376
DOI: 10.1021/BI300870G
Page generated: Mon Oct 7 17:49:58 2024
|