Sodium in PDB 4o0c: High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein
Enzymatic activity of High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein
All present enzymatic activity of High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein:
3.4.19.5;
3.5.1.1;
Protein crystallography data
The structure of High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein, PDB code: 4o0c
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)
|
29.04 /
1.50
|
Space group
|
P 65
|
Cell size a, b, c (Å), α, β, γ (°)
|
59.213,
59.213,
297.793,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
15.2 /
20.5
|
Other elements in 4o0c:
The structure of High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein
(pdb code 4o0c). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 5 binding sites of Sodium where determined in the
High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein, PDB code: 4o0c:
Jump to Sodium binding site number:
1;
2;
3;
4;
5;
Sodium binding site 1 out
of 5 in 4o0c
Go back to
Sodium Binding Sites List in 4o0c
Sodium binding site 1 out
of 5 in the High Resolution Crystal Structure of Uncleaved 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 High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na401
b:16.0
occ:1.00
|
O
|
A:ALA63
|
2.3
|
14.3
|
1.0
|
O
|
A:ASP58
|
2.4
|
17.1
|
1.0
|
O
|
A:CYS65
|
2.4
|
16.6
|
1.0
|
O
|
A:GLU56
|
2.5
|
17.4
|
1.0
|
O
|
A:LEU55
|
2.6
|
15.4
|
1.0
|
O
|
A:PHE61
|
2.7
|
14.7
|
1.0
|
C
|
A:GLU56
|
3.2
|
13.1
|
1.0
|
C
|
A:ASP58
|
3.3
|
16.0
|
1.0
|
C
|
A:CYS65
|
3.5
|
14.9
|
1.0
|
C
|
A:ALA63
|
3.5
|
13.9
|
1.0
|
CA
|
A:GLU56
|
3.6
|
13.8
|
1.0
|
C
|
A:PHE61
|
3.7
|
13.5
|
1.0
|
C
|
A:LEU55
|
3.7
|
13.2
|
1.0
|
N
|
A:ASP58
|
3.9
|
16.5
|
1.0
|
N
|
A:PHE61
|
4.0
|
15.2
|
1.0
|
CB
|
A:PHE61
|
4.0
|
16.5
|
1.0
|
N
|
A:PRO59
|
4.1
|
18.5
|
1.0
|
N
|
A:ALA63
|
4.1
|
14.9
|
1.0
|
CA
|
A:PHE61
|
4.1
|
15.1
|
1.0
|
N
|
A:GLU56
|
4.1
|
13.3
|
1.0
|
CA
|
A:PRO59
|
4.2
|
18.7
|
1.0
|
N
|
A:CYS65
|
4.2
|
16.4
|
1.0
|
CA
|
A:ASP58
|
4.2
|
15.0
|
1.0
|
N
|
A:ASP57
|
4.2
|
15.2
|
1.0
|
CA
|
A:ALA63
|
4.3
|
13.1
|
1.0
|
N
|
A:GLY66
|
4.3
|
14.4
|
1.0
|
CA
|
A:GLY66
|
4.3
|
15.5
|
1.0
|
C
|
A:GLY64
|
4.3
|
15.5
|
1.0
|
CA
|
A:CYS65
|
4.3
|
14.6
|
1.0
|
C
|
A:ASP57
|
4.5
|
16.3
|
1.0
|
N
|
A:GLY64
|
4.5
|
13.2
|
1.0
|
C
|
A:PRO59
|
4.5
|
16.3
|
1.0
|
CB
|
A:ALA63
|
4.6
|
12.7
|
1.0
|
CA
|
A:GLY64
|
4.7
|
15.5
|
1.0
|
O
|
A:GLY64
|
4.7
|
16.2
|
1.0
|
CB
|
A:ASP58
|
4.8
|
16.0
|
1.0
|
C
|
A:GLY66
|
4.8
|
16.6
|
1.0
|
CA
|
A:ASP57
|
4.8
|
16.9
|
1.0
|
N
|
A:ASN62
|
4.8
|
12.8
|
1.0
|
CB
|
A:CYS65
|
4.9
|
14.1
|
1.0
|
N
|
A:GLU60
|
4.9
|
16.2
|
1.0
|
N
|
A:SER67
|
4.9
|
18.5
|
1.0
|
O
|
A:PRO59
|
5.0
|
19.0
|
1.0
|
CB
|
A:GLU56
|
5.0
|
12.1
|
1.0
|
|
Sodium binding site 2 out
of 5 in 4o0c
Go back to
Sodium Binding Sites List in 4o0c
Sodium binding site 2 out
of 5 in the High Resolution Crystal Structure of Uncleaved 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 High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na402
b:20.8
occ:1.00
|
O
|
A:HOH646
|
2.8
|
21.3
|
1.0
|
O
|
A:HOH639
|
3.0
|
17.2
|
1.0
|
N
|
A:GLY10
|
3.4
|
14.9
|
1.0
|
CD2
|
A:PHE61
|
3.8
|
15.4
|
1.0
|
CG
|
A:PRO284
|
4.0
|
16.4
|
1.0
|
CE2
|
A:PHE61
|
4.0
|
14.9
|
1.0
|
CA
|
A:GLY9
|
4.0
|
17.6
|
1.0
|
C
|
A:GLY9
|
4.2
|
16.4
|
1.0
|
CA
|
A:GLY10
|
4.2
|
14.8
|
1.0
|
CD
|
A:PRO284
|
4.4
|
14.7
|
1.0
|
NH2
|
A:ARG19
|
4.6
|
23.1
|
1.0
|
O
|
A:GLY10
|
4.7
|
16.0
|
1.0
|
CB
|
A:PRO284
|
4.7
|
15.2
|
1.0
|
CG
|
A:PHE61
|
4.9
|
16.2
|
1.0
|
O
|
A:GLU60
|
4.9
|
17.9
|
1.0
|
O
|
A:GLY167
|
4.9
|
19.5
|
1.0
|
|
Sodium binding site 3 out
of 5 in 4o0c
Go back to
Sodium Binding Sites List in 4o0c
Sodium binding site 3 out
of 5 in the High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 3 of High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na401
b:16.7
occ:1.00
|
O
|
B:CYS65
|
2.2
|
16.8
|
1.0
|
O
|
B:ALA63
|
2.2
|
16.8
|
1.0
|
O
|
B:ASP58
|
2.3
|
17.6
|
1.0
|
O
|
B:LEU55
|
2.4
|
15.5
|
1.0
|
O
|
B:GLU56
|
2.5
|
16.4
|
1.0
|
O
|
B:PHE61
|
2.6
|
19.6
|
1.0
|
C
|
B:GLU56
|
3.2
|
15.5
|
1.0
|
C
|
B:CYS65
|
3.3
|
17.1
|
1.0
|
C
|
B:ASP58
|
3.3
|
15.4
|
1.0
|
C
|
B:ALA63
|
3.5
|
15.2
|
1.0
|
C
|
B:LEU55
|
3.5
|
13.7
|
1.0
|
CA
|
B:GLU56
|
3.5
|
11.6
|
1.0
|
C
|
B:PHE61
|
3.6
|
16.4
|
1.0
|
N
|
B:CYS65
|
3.7
|
18.0
|
1.0
|
N
|
B:ALA63
|
3.9
|
14.9
|
1.0
|
N
|
B:ASP58
|
3.9
|
14.5
|
1.0
|
N
|
B:GLU56
|
3.9
|
12.4
|
1.0
|
CA
|
B:CYS65
|
4.0
|
17.2
|
1.0
|
CB
|
B:PHE61
|
4.1
|
17.7
|
1.0
|
C
|
B:GLY64
|
4.1
|
15.3
|
1.0
|
CA
|
B:ASP58
|
4.1
|
14.1
|
1.0
|
CA
|
B:PHE61
|
4.1
|
17.1
|
1.0
|
N
|
B:PHE61
|
4.2
|
18.4
|
1.0
|
CA
|
B:PRO59
|
4.2
|
17.2
|
1.0
|
N
|
B:ASP57
|
4.2
|
14.8
|
1.0
|
C
|
B:ASP57
|
4.2
|
14.6
|
1.0
|
N
|
B:PRO59
|
4.3
|
16.8
|
1.0
|
CA
|
B:ALA63
|
4.3
|
14.3
|
1.0
|
N
|
B:GLY66
|
4.3
|
16.7
|
1.0
|
N
|
B:GLY64
|
4.4
|
14.0
|
1.0
|
CA
|
B:GLY66
|
4.5
|
18.0
|
1.0
|
CA
|
B:GLY64
|
4.5
|
15.9
|
1.0
|
CB
|
B:CYS65
|
4.5
|
18.8
|
1.0
|
C
|
B:PRO59
|
4.6
|
16.8
|
1.0
|
CB
|
B:ASP58
|
4.7
|
15.0
|
1.0
|
N
|
B:ASN62
|
4.7
|
15.0
|
1.0
|
O
|
B:ASP57
|
4.7
|
17.5
|
1.0
|
CA
|
B:ASP57
|
4.7
|
15.1
|
1.0
|
O
|
B:GLY64
|
4.7
|
15.7
|
1.0
|
CA
|
B:LEU55
|
4.8
|
14.1
|
1.0
|
CB
|
B:ALA63
|
4.8
|
17.5
|
1.0
|
C
|
B:GLY66
|
4.9
|
16.6
|
1.0
|
O
|
B:PRO59
|
4.9
|
17.3
|
1.0
|
CB
|
B:GLU56
|
4.9
|
14.4
|
1.0
|
C
|
B:ASN62
|
5.0
|
14.9
|
1.0
|
N
|
B:GLU60
|
5.0
|
15.9
|
1.0
|
|
Sodium binding site 4 out
of 5 in 4o0c
Go back to
Sodium Binding Sites List in 4o0c
Sodium binding site 4 out
of 5 in the High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 4 of High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na402
b:16.2
occ:1.00
|
O
|
B:HOH540
|
2.3
|
18.6
|
1.0
|
O
|
B:MET109
|
2.4
|
17.0
|
1.0
|
O
|
B:HIS114
|
2.4
|
14.6
|
1.0
|
O
|
B:THR112
|
2.5
|
15.0
|
1.0
|
O
|
B:VAL108
|
2.8
|
15.0
|
1.0
|
C
|
B:MET109
|
3.2
|
15.5
|
1.0
|
C
|
B:HIS114
|
3.5
|
14.6
|
1.0
|
CA
|
B:MET109
|
3.5
|
15.6
|
1.0
|
N
|
B:HIS114
|
3.6
|
14.8
|
1.0
|
C
|
B:THR112
|
3.6
|
16.1
|
1.0
|
OG1
|
B:THR112
|
3.7
|
16.5
|
1.0
|
C
|
B:VAL108
|
3.8
|
14.7
|
1.0
|
C
|
B:PRO113
|
3.9
|
16.3
|
1.0
|
CA
|
B:HIS114
|
4.1
|
14.2
|
1.0
|
N
|
B:MET109
|
4.2
|
14.8
|
1.0
|
CA
|
B:PRO113
|
4.3
|
15.2
|
1.0
|
N
|
B:THR112
|
4.3
|
15.3
|
1.0
|
N
|
B:GLU110
|
4.4
|
15.6
|
1.0
|
NA
|
B:NA403
|
4.4
|
21.7
|
1.0
|
N
|
B:PRO113
|
4.4
|
15.0
|
1.0
|
CA
|
B:THR112
|
4.4
|
14.5
|
1.0
|
O
|
B:PRO113
|
4.4
|
15.7
|
1.0
|
N
|
B:CYS115
|
4.5
|
14.3
|
1.0
|
O
|
B:ALA89
|
4.5
|
13.7
|
1.0
|
CB
|
B:THR112
|
4.7
|
15.3
|
1.0
|
CA
|
B:CYS115
|
4.8
|
13.6
|
1.0
|
CB
|
B:MET109
|
4.8
|
15.7
|
1.0
|
O
|
A:HOH664
|
4.9
|
23.1
|
1.0
|
CG
|
B:MET109
|
5.0
|
16.7
|
1.0
|
|
Sodium binding site 5 out
of 5 in 4o0c
Go back to
Sodium Binding Sites List in 4o0c
Sodium binding site 5 out
of 5 in the High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 5 of High Resolution Crystal Structure of Uncleaved Human L-Asparaginase Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na403
b:21.7
occ:1.00
|
O
|
A:HOH664
|
2.5
|
23.1
|
1.0
|
O
|
B:HOH540
|
2.6
|
18.6
|
1.0
|
CA
|
B:SER88
|
3.5
|
14.8
|
1.0
|
OG
|
B:SER88
|
3.7
|
17.0
|
1.0
|
CB
|
B:SER88
|
3.7
|
16.1
|
1.0
|
NZ
|
A:LYS227
|
3.8
|
14.9
|
1.0
|
CD
|
A:LYS227
|
3.8
|
14.2
|
1.0
|
N
|
B:ALA89
|
3.9
|
14.1
|
1.0
|
SG
|
B:CYS115
|
3.9
|
18.2
|
1.0
|
CE
|
A:LYS227
|
4.1
|
15.3
|
1.0
|
O
|
B:HOH571
|
4.1
|
17.9
|
1.0
|
O
|
A:HOH674
|
4.3
|
24.8
|
1.0
|
C
|
B:SER88
|
4.3
|
14.8
|
1.0
|
NA
|
B:NA402
|
4.4
|
16.2
|
1.0
|
O
|
B:ALA89
|
4.4
|
13.7
|
1.0
|
N
|
B:SER88
|
4.6
|
13.4
|
1.0
|
CG
|
A:LYS227
|
4.9
|
15.5
|
1.0
|
O
|
B:LEU87
|
4.9
|
12.4
|
1.0
|
CG
|
B:MET109
|
5.0
|
16.7
|
1.0
|
|
Reference:
J.Nomme,
Y.Su,
A.Lavie.
Elucidation of the Specific Function of the Conserved Threonine Triad Responsible For Human L-Asparaginase Autocleavage and Substrate Hydrolysis. J.Mol.Biol. V. 426 2471 2014.
ISSN: ISSN 0022-2836
PubMed: 24768817
DOI: 10.1016/J.JMB.2014.04.016
Page generated: Mon Oct 7 17:20:43 2024
|