Iron in PDB 1ohv: 4-Aminobutyrate-Aminotransferase From Pig
Enzymatic activity of 4-Aminobutyrate-Aminotransferase From Pig
All present enzymatic activity of 4-Aminobutyrate-Aminotransferase From Pig:
2.6.1.19;
Protein crystallography data
The structure of 4-Aminobutyrate-Aminotransferase From Pig, PDB code: 1ohv
was solved by
P.Storici,
T.Schirmer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
2.3
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
68.597,
225.045,
70.349,
90.00,
108.39,
90.00
|
R / Rfree (%)
|
18.8 /
22.1
|
Iron Binding Sites:
The binding sites of Iron atom in the 4-Aminobutyrate-Aminotransferase From Pig
(pdb code 1ohv). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
4-Aminobutyrate-Aminotransferase From Pig, PDB code: 1ohv:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 1ohv
Go back to
Iron Binding Sites List in 1ohv
Iron binding site 1 out
of 4 in the 4-Aminobutyrate-Aminotransferase From Pig
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of 4-Aminobutyrate-Aminotransferase From Pig within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe800
b:13.5
occ:1.00
|
FE1
|
A:FES800
|
0.0
|
13.5
|
1.0
|
SG
|
A:CYS138
|
2.2
|
15.9
|
1.0
|
S2
|
A:FES800
|
2.3
|
14.7
|
1.0
|
SG
|
A:CYS135
|
2.3
|
12.2
|
1.0
|
S1
|
A:FES800
|
2.3
|
14.5
|
1.0
|
FE2
|
A:FES800
|
2.5
|
14.5
|
1.0
|
CB
|
A:CYS138
|
3.2
|
14.2
|
1.0
|
CB
|
A:CYS135
|
3.4
|
13.7
|
1.0
|
N
|
A:CYS138
|
3.7
|
14.2
|
1.0
|
N
|
A:CYS135
|
3.8
|
14.1
|
1.0
|
CA
|
A:CYS138
|
4.0
|
14.2
|
1.0
|
CA
|
A:CYS135
|
4.1
|
13.8
|
1.0
|
SG
|
B:CYS135
|
4.3
|
12.7
|
1.0
|
SG
|
B:CYS138
|
4.5
|
16.5
|
1.0
|
C
|
A:ALA134
|
4.5
|
14.4
|
1.0
|
C
|
A:CYS135
|
4.6
|
13.9
|
1.0
|
CB
|
A:ALA134
|
4.6
|
14.9
|
1.0
|
O
|
A:CYS135
|
4.6
|
13.9
|
1.0
|
O
|
A:HOH2057
|
4.8
|
27.4
|
1.0
|
O
|
A:HOH2165
|
4.8
|
16.5
|
1.0
|
O
|
A:HOH2060
|
4.8
|
25.0
|
1.0
|
N
|
A:ALA134
|
4.8
|
14.6
|
1.0
|
C
|
A:SER137
|
4.9
|
14.2
|
1.0
|
CA
|
A:ALA134
|
4.9
|
14.5
|
1.0
|
|
Iron binding site 2 out
of 4 in 1ohv
Go back to
Iron Binding Sites List in 1ohv
Iron binding site 2 out
of 4 in the 4-Aminobutyrate-Aminotransferase From Pig
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of 4-Aminobutyrate-Aminotransferase From Pig within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe800
b:14.5
occ:1.00
|
FE2
|
A:FES800
|
0.0
|
14.5
|
1.0
|
SG
|
B:CYS138
|
2.3
|
16.5
|
1.0
|
S2
|
A:FES800
|
2.3
|
14.7
|
1.0
|
SG
|
B:CYS135
|
2.3
|
12.7
|
1.0
|
S1
|
A:FES800
|
2.3
|
14.5
|
1.0
|
FE1
|
A:FES800
|
2.5
|
13.5
|
1.0
|
CB
|
B:CYS138
|
3.2
|
14.3
|
1.0
|
CB
|
B:CYS135
|
3.5
|
13.9
|
1.0
|
N
|
B:CYS138
|
3.8
|
13.9
|
1.0
|
N
|
B:CYS135
|
3.8
|
14.2
|
1.0
|
CA
|
B:CYS138
|
4.1
|
14.3
|
1.0
|
CA
|
B:CYS135
|
4.1
|
13.9
|
1.0
|
SG
|
A:CYS135
|
4.2
|
12.2
|
1.0
|
SG
|
A:CYS138
|
4.4
|
15.9
|
1.0
|
C
|
B:ALA134
|
4.5
|
14.4
|
1.0
|
CB
|
B:ALA134
|
4.6
|
14.7
|
1.0
|
C
|
B:CYS135
|
4.6
|
13.9
|
1.0
|
O
|
B:CYS135
|
4.7
|
14.0
|
1.0
|
O
|
B:HOH2147
|
4.8
|
22.3
|
1.0
|
O
|
A:HOH2060
|
4.8
|
25.0
|
1.0
|
N
|
B:ALA134
|
4.9
|
14.5
|
1.0
|
CA
|
B:ALA134
|
4.9
|
14.6
|
1.0
|
C
|
B:SER137
|
4.9
|
14.1
|
1.0
|
CB
|
A:CYS138
|
5.0
|
14.2
|
1.0
|
|
Iron binding site 3 out
of 4 in 1ohv
Go back to
Iron Binding Sites List in 1ohv
Iron binding site 3 out
of 4 in the 4-Aminobutyrate-Aminotransferase From Pig
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of 4-Aminobutyrate-Aminotransferase From Pig within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe800
b:13.9
occ:1.00
|
FE1
|
C:FES800
|
0.0
|
13.9
|
1.0
|
S1
|
C:FES800
|
2.2
|
10.8
|
1.0
|
SG
|
D:CYS135
|
2.3
|
12.4
|
1.0
|
SG
|
D:CYS138
|
2.3
|
16.3
|
1.0
|
S2
|
C:FES800
|
2.3
|
15.8
|
1.0
|
FE2
|
C:FES800
|
2.6
|
14.6
|
1.0
|
CB
|
D:CYS138
|
3.3
|
14.2
|
1.0
|
CB
|
D:CYS135
|
3.4
|
13.8
|
1.0
|
N
|
D:CYS135
|
3.8
|
14.1
|
1.0
|
N
|
D:CYS138
|
3.8
|
14.0
|
1.0
|
CA
|
D:CYS135
|
4.1
|
13.8
|
1.0
|
CA
|
D:CYS138
|
4.1
|
14.2
|
1.0
|
SG
|
C:CYS135
|
4.2
|
12.6
|
1.0
|
C
|
D:ALA134
|
4.5
|
14.4
|
1.0
|
CB
|
D:ALA134
|
4.5
|
14.7
|
1.0
|
SG
|
C:CYS138
|
4.5
|
16.4
|
1.0
|
O
|
D:HOH2135
|
4.6
|
30.7
|
1.0
|
C
|
D:CYS135
|
4.6
|
13.9
|
1.0
|
O
|
D:CYS135
|
4.7
|
14.0
|
1.0
|
N
|
D:ALA134
|
4.8
|
14.4
|
1.0
|
CA
|
D:ALA134
|
4.8
|
14.5
|
1.0
|
O
|
D:HOH2171
|
4.9
|
26.1
|
1.0
|
C
|
D:SER137
|
5.0
|
14.1
|
1.0
|
|
Iron binding site 4 out
of 4 in 1ohv
Go back to
Iron Binding Sites List in 1ohv
Iron binding site 4 out
of 4 in the 4-Aminobutyrate-Aminotransferase From Pig
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of 4-Aminobutyrate-Aminotransferase From Pig within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe800
b:14.6
occ:1.00
|
FE2
|
C:FES800
|
0.0
|
14.6
|
1.0
|
SG
|
C:CYS138
|
2.3
|
16.4
|
1.0
|
SG
|
C:CYS135
|
2.3
|
12.6
|
1.0
|
S1
|
C:FES800
|
2.3
|
10.8
|
1.0
|
S2
|
C:FES800
|
2.3
|
15.8
|
1.0
|
FE1
|
C:FES800
|
2.6
|
13.9
|
1.0
|
CB
|
C:CYS138
|
3.2
|
14.1
|
1.0
|
CB
|
C:CYS135
|
3.4
|
13.8
|
1.0
|
N
|
C:CYS138
|
3.8
|
13.9
|
1.0
|
N
|
C:CYS135
|
3.8
|
14.0
|
1.0
|
CA
|
C:CYS138
|
4.1
|
14.3
|
1.0
|
CA
|
C:CYS135
|
4.1
|
13.8
|
1.0
|
SG
|
D:CYS135
|
4.2
|
12.4
|
1.0
|
C
|
C:ALA134
|
4.5
|
14.4
|
1.0
|
O
|
C:HOH2117
|
4.5
|
15.2
|
1.0
|
SG
|
D:CYS138
|
4.5
|
16.3
|
1.0
|
CB
|
C:ALA134
|
4.5
|
14.9
|
1.0
|
C
|
C:CYS135
|
4.6
|
13.9
|
1.0
|
O
|
C:CYS135
|
4.7
|
14.1
|
1.0
|
N
|
C:ALA134
|
4.8
|
14.7
|
1.0
|
CA
|
C:ALA134
|
4.8
|
14.6
|
1.0
|
O
|
C:HOH2147
|
4.9
|
35.3
|
1.0
|
C
|
C:SER137
|
4.9
|
14.1
|
1.0
|
|
Reference:
P.Storici,
D.De Biase,
F.Bossa,
S.Bruno,
A.Mozzarelli,
C.Peneff,
R.Silverman,
T.Schirmer.
Structures of {Gamma}-Aminobutyric Acid (Gaba) Aminotransferase, A Pyridoxal 5'-Phosphate, and [2FE-2S] Cluster-Containing Enzyme, Complexed with {Gamma}-Ethynyl-Gaba and with the Antiepilepsy Drug Vigabatrin J.Biol.Chem. V. 279 363 2004.
ISSN: ISSN 0021-9258
PubMed: 14534310
DOI: 10.1074/JBC.M305884200
Page generated: Sat Aug 3 12:29:05 2024
|