Manganese in PDB 1yny: Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition
Enzymatic activity of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition
All present enzymatic activity of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition:
3.5.2.2;
Protein crystallography data
The structure of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition, PDB code: 1yny
was solved by
K.V.Radha Kishan,
R.M.Vohra,
K.Ganeshan,
V.Agrawal,
V.M.Sharma,
R.Sharma,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
2.30
|
Space group
|
P 64
|
Cell size a, b, c (Å), α, β, γ (°)
|
129.540,
129.540,
102.850,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
19.9 /
24.3
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition
(pdb code 1yny). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the
Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition, PDB code: 1yny:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 1yny
Go back to
Manganese Binding Sites List in 1yny
Manganese binding site 1 out
of 4 in the Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn471
b:18.0
occ:1.00
|
NE2
|
A:HIS58
|
2.1
|
17.5
|
1.0
|
O
|
A:HOH1128
|
2.1
|
12.1
|
1.0
|
NE2
|
A:HIS60
|
2.2
|
21.1
|
1.0
|
OD1
|
A:ASP315
|
2.3
|
14.2
|
1.0
|
CE1
|
A:HIS58
|
3.0
|
16.3
|
1.0
|
CD2
|
A:HIS58
|
3.1
|
16.0
|
1.0
|
CE1
|
A:HIS60
|
3.2
|
18.6
|
1.0
|
CD2
|
A:HIS60
|
3.2
|
18.4
|
1.0
|
CG
|
A:ASP315
|
3.2
|
15.3
|
1.0
|
NZ
|
A:LYS150
|
3.3
|
12.3
|
1.0
|
MN
|
A:MN472
|
3.4
|
17.8
|
1.0
|
OD2
|
A:ASP315
|
3.7
|
12.8
|
1.0
|
O
|
A:HOH1112
|
3.9
|
18.5
|
1.0
|
O
|
A:HOH1093
|
4.0
|
22.7
|
1.0
|
ND1
|
A:HIS58
|
4.2
|
15.6
|
1.0
|
CG
|
A:HIS58
|
4.2
|
15.5
|
1.0
|
ND1
|
A:HIS60
|
4.3
|
17.5
|
1.0
|
CG
|
A:HIS60
|
4.3
|
18.4
|
1.0
|
CB
|
A:ASP315
|
4.3
|
14.7
|
1.0
|
CD2
|
A:HIS239
|
4.4
|
15.8
|
1.0
|
CE2
|
A:PHE92
|
4.5
|
11.1
|
1.0
|
NE2
|
A:HIS239
|
4.5
|
14.7
|
1.0
|
CD2
|
A:PHE92
|
4.6
|
11.7
|
1.0
|
CA
|
A:ASP315
|
4.8
|
15.2
|
1.0
|
CE
|
A:LYS150
|
4.8
|
15.0
|
1.0
|
|
Manganese binding site 2 out
of 4 in 1yny
Go back to
Manganese Binding Sites List in 1yny
Manganese binding site 2 out
of 4 in the Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn472
b:17.8
occ:1.00
|
O
|
A:HOH1128
|
2.1
|
12.1
|
1.0
|
ND1
|
A:HIS183
|
2.3
|
15.4
|
1.0
|
NE2
|
A:HIS239
|
2.3
|
14.7
|
1.0
|
O
|
A:HOH1112
|
2.5
|
18.5
|
1.0
|
CE1
|
A:HIS183
|
3.0
|
16.9
|
1.0
|
CD2
|
A:HIS239
|
3.2
|
15.8
|
1.0
|
CE1
|
A:HIS239
|
3.3
|
14.9
|
1.0
|
CG
|
A:HIS183
|
3.4
|
15.1
|
1.0
|
NZ
|
A:LYS150
|
3.4
|
12.3
|
1.0
|
MN
|
A:MN471
|
3.4
|
18.0
|
1.0
|
CB
|
A:HIS183
|
3.8
|
10.6
|
1.0
|
O
|
A:SER288
|
3.9
|
14.1
|
1.0
|
OH
|
A:TYR155
|
4.1
|
17.5
|
1.0
|
NE2
|
A:HIS183
|
4.2
|
17.0
|
1.0
|
CE
|
A:LYS150
|
4.3
|
15.0
|
1.0
|
CE2
|
A:PHE152
|
4.4
|
15.5
|
1.0
|
CD2
|
A:HIS183
|
4.4
|
16.3
|
1.0
|
CG
|
A:HIS239
|
4.4
|
16.2
|
1.0
|
ND1
|
A:HIS239
|
4.4
|
15.9
|
1.0
|
CG2
|
A:VAL238
|
4.6
|
11.3
|
1.0
|
CE1
|
A:HIS58
|
4.6
|
16.3
|
1.0
|
NE2
|
A:HIS58
|
4.6
|
17.5
|
1.0
|
OD2
|
A:ASP315
|
4.7
|
12.8
|
1.0
|
O
|
A:HOH1093
|
4.7
|
22.7
|
1.0
|
CA
|
A:HIS183
|
4.7
|
10.5
|
1.0
|
CE2
|
A:TYR155
|
4.8
|
21.4
|
1.0
|
OD1
|
A:ASP315
|
4.9
|
14.2
|
1.0
|
CD2
|
A:PHE152
|
4.9
|
14.4
|
1.0
|
CZ
|
A:TYR155
|
5.0
|
18.9
|
1.0
|
C
|
A:SER288
|
5.0
|
14.2
|
1.0
|
|
Manganese binding site 3 out
of 4 in 1yny
Go back to
Manganese Binding Sites List in 1yny
Manganese binding site 3 out
of 4 in the Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn471
b:17.1
occ:1.00
|
O
|
B:HOH5110
|
2.1
|
19.3
|
1.0
|
NE2
|
B:HIS58
|
2.2
|
18.2
|
1.0
|
NE2
|
B:HIS60
|
2.2
|
17.1
|
1.0
|
OD1
|
B:ASP315
|
2.3
|
14.2
|
1.0
|
CD2
|
B:HIS58
|
3.1
|
17.9
|
1.0
|
CD2
|
B:HIS60
|
3.1
|
15.2
|
1.0
|
NZ
|
B:LYS150
|
3.2
|
11.6
|
1.0
|
CE1
|
B:HIS58
|
3.3
|
17.4
|
1.0
|
CE1
|
B:HIS60
|
3.3
|
16.9
|
1.0
|
CG
|
B:ASP315
|
3.3
|
14.0
|
1.0
|
MN
|
B:MN472
|
3.5
|
15.3
|
1.0
|
OD2
|
B:ASP315
|
3.8
|
14.6
|
1.0
|
O
|
B:HOH5109
|
4.0
|
31.0
|
1.0
|
O
|
B:HOH5084
|
4.0
|
20.2
|
1.0
|
CG
|
B:HIS58
|
4.3
|
14.6
|
1.0
|
CG
|
B:HIS60
|
4.3
|
16.4
|
1.0
|
ND1
|
B:HIS58
|
4.3
|
15.6
|
1.0
|
ND1
|
B:HIS60
|
4.3
|
18.0
|
1.0
|
CE2
|
B:PHE92
|
4.4
|
10.8
|
1.0
|
CB
|
B:ASP315
|
4.4
|
13.3
|
1.0
|
CD2
|
B:HIS239
|
4.4
|
12.1
|
1.0
|
CD2
|
B:PHE92
|
4.5
|
12.2
|
1.0
|
NE2
|
B:HIS239
|
4.6
|
10.1
|
1.0
|
CA
|
B:ASP315
|
4.7
|
14.1
|
1.0
|
CE
|
B:LYS150
|
4.7
|
16.6
|
1.0
|
|
Manganese binding site 4 out
of 4 in 1yny
Go back to
Manganese Binding Sites List in 1yny
Manganese binding site 4 out
of 4 in the Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Molecular Structure of D-Hydantoinase From A Bacillus Sp. AR9: Evidence For Mercury Inhibition within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn472
b:15.3
occ:1.00
|
O
|
B:HOH5110
|
2.1
|
19.3
|
1.0
|
ND1
|
B:HIS183
|
2.3
|
11.9
|
1.0
|
O
|
B:HOH5109
|
2.3
|
31.0
|
1.0
|
NE2
|
B:HIS239
|
2.3
|
10.1
|
1.0
|
CE1
|
B:HIS183
|
3.1
|
11.4
|
1.0
|
CD2
|
B:HIS239
|
3.3
|
12.1
|
1.0
|
CE1
|
B:HIS239
|
3.3
|
10.6
|
1.0
|
NZ
|
B:LYS150
|
3.4
|
11.6
|
1.0
|
CG
|
B:HIS183
|
3.4
|
12.7
|
1.0
|
MN
|
B:MN471
|
3.5
|
17.1
|
1.0
|
CB
|
B:HIS183
|
3.8
|
11.6
|
1.0
|
O
|
B:SER288
|
3.9
|
15.7
|
1.0
|
CE2
|
B:PHE152
|
4.2
|
14.5
|
1.0
|
NE2
|
B:HIS183
|
4.3
|
11.6
|
1.0
|
OH
|
B:TYR155
|
4.3
|
21.5
|
1.0
|
CE
|
B:LYS150
|
4.3
|
16.6
|
1.0
|
CD2
|
B:HIS183
|
4.4
|
13.3
|
1.0
|
CG
|
B:HIS239
|
4.4
|
13.1
|
1.0
|
ND1
|
B:HIS239
|
4.4
|
13.1
|
1.0
|
CG2
|
B:VAL238
|
4.5
|
9.5
|
1.0
|
NE2
|
B:HIS58
|
4.6
|
18.2
|
1.0
|
CE1
|
B:HIS58
|
4.7
|
17.4
|
1.0
|
OD2
|
B:ASP315
|
4.7
|
14.6
|
1.0
|
CA
|
B:HIS183
|
4.8
|
10.5
|
1.0
|
O
|
B:HOH5084
|
4.8
|
20.2
|
1.0
|
OD1
|
B:ASP315
|
4.8
|
14.2
|
1.0
|
CE2
|
B:TYR155
|
4.9
|
23.6
|
1.0
|
CD2
|
B:PHE152
|
4.9
|
15.7
|
1.0
|
|
Reference:
K.V.Radha Kishan,
R.M.Vohra,
K.Ganesan,
V.Agrawal,
V.M.Sharma,
R.Sharma.
Molecular Structure of D-Hydantoinase From Bacillus Sp. AR9: Evidence For Mercury Inhibition. J.Mol.Biol. V. 347 95 2005.
ISSN: ISSN 0022-2836
PubMed: 15733920
DOI: 10.1016/J.JMB.2005.01.025
Page generated: Sat Oct 5 13:13:17 2024
|