Iron in PDB 1b9r: Terpredoxin From Pseudomonas Sp.
Iron Binding Sites:
The binding sites of Iron atom in the Terpredoxin From Pseudomonas Sp.
(pdb code 1b9r). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Terpredoxin From Pseudomonas Sp., PDB code: 1b9r:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 1b9r
Go back to
Iron Binding Sites List in 1b9r
Iron binding site 1 out
of 2 in the Terpredoxin From Pseudomonas Sp.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Terpredoxin From Pseudomonas Sp. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe106
b:0.0
occ:1.00
|
FE1
|
A:FES106
|
0.0
|
0.0
|
1.0
|
S1
|
A:FES106
|
2.2
|
0.0
|
1.0
|
SG
|
A:CYS39
|
2.2
|
0.0
|
1.0
|
S2
|
A:FES106
|
2.2
|
0.0
|
1.0
|
SG
|
A:CYS45
|
2.2
|
0.0
|
1.0
|
FE2
|
A:FES106
|
2.7
|
0.0
|
1.0
|
H
|
A:CYS39
|
3.0
|
0.0
|
1.0
|
H
|
A:CYS45
|
3.1
|
0.0
|
1.0
|
HB3
|
A:CYS39
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS39
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS45
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS45
|
3.3
|
0.0
|
1.0
|
HB2
|
A:GLU38
|
3.4
|
0.0
|
1.0
|
H
|
A:GLY41
|
3.6
|
0.0
|
1.0
|
O
|
A:CYS45
|
3.7
|
0.0
|
1.0
|
N
|
A:CYS39
|
3.8
|
0.0
|
1.0
|
N
|
A:CYS45
|
3.8
|
0.0
|
1.0
|
CA
|
A:CYS45
|
3.8
|
0.0
|
1.0
|
C
|
A:CYS45
|
3.9
|
0.0
|
1.0
|
H
|
A:VAL44
|
3.9
|
0.0
|
1.0
|
OE1
|
A:GLU38
|
4.0
|
0.0
|
1.0
|
CA
|
A:CYS39
|
4.1
|
0.0
|
1.0
|
H
|
A:GLY40
|
4.1
|
0.0
|
1.0
|
SG
|
A:CYS48
|
4.1
|
0.0
|
1.0
|
H
|
A:CYS43
|
4.1
|
0.0
|
1.0
|
HB2
|
A:CYS39
|
4.2
|
0.0
|
1.0
|
HB3
|
A:GLU38
|
4.2
|
0.0
|
1.0
|
HB2
|
A:CYS45
|
4.2
|
0.0
|
1.0
|
HB3
|
A:CYS48
|
4.3
|
0.0
|
1.0
|
SG
|
A:CYS86
|
4.3
|
0.0
|
1.0
|
CB
|
A:GLU38
|
4.3
|
0.0
|
1.0
|
HG11
|
A:VAL44
|
4.5
|
0.0
|
1.0
|
HA
|
A:CYS43
|
4.5
|
0.0
|
1.0
|
H
|
A:THR47
|
4.5
|
0.0
|
1.0
|
N
|
A:GLY41
|
4.6
|
0.0
|
1.0
|
N
|
A:GLY40
|
4.6
|
0.0
|
1.0
|
HA2
|
A:GLY41
|
4.6
|
0.0
|
1.0
|
H
|
A:CYS48
|
4.7
|
0.0
|
1.0
|
C
|
A:CYS39
|
4.7
|
0.0
|
1.0
|
N
|
A:ALA46
|
4.7
|
0.0
|
1.0
|
N
|
A:VAL44
|
4.7
|
0.0
|
1.0
|
HD23
|
A:LEU84
|
4.8
|
0.0
|
1.0
|
CB
|
A:CYS48
|
4.8
|
0.0
|
1.0
|
C
|
A:GLU38
|
4.9
|
0.0
|
1.0
|
HA
|
A:CYS45
|
4.9
|
0.0
|
1.0
|
N
|
A:CYS43
|
4.9
|
0.0
|
1.0
|
HA
|
A:ALA46
|
4.9
|
0.0
|
1.0
|
H
|
A:SER42
|
5.0
|
0.0
|
1.0
|
|
Iron binding site 2 out
of 2 in 1b9r
Go back to
Iron Binding Sites List in 1b9r
Iron binding site 2 out
of 2 in the Terpredoxin From Pseudomonas Sp.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Terpredoxin From Pseudomonas Sp. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe106
b:0.0
occ:1.00
|
FE2
|
A:FES106
|
0.0
|
0.0
|
1.0
|
SG
|
A:CYS48
|
2.2
|
0.0
|
1.0
|
SG
|
A:CYS86
|
2.2
|
0.0
|
1.0
|
S1
|
A:FES106
|
2.2
|
0.0
|
1.0
|
S2
|
A:FES106
|
2.2
|
0.0
|
1.0
|
FE1
|
A:FES106
|
2.7
|
0.0
|
1.0
|
HB3
|
A:CYS86
|
3.1
|
0.0
|
1.0
|
HB3
|
A:CYS48
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS48
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS86
|
3.3
|
0.0
|
1.0
|
HB2
|
A:CYS48
|
3.7
|
0.0
|
1.0
|
HB3
|
A:LEU84
|
3.7
|
0.0
|
1.0
|
HD23
|
A:LEU84
|
3.7
|
0.0
|
1.0
|
HD22
|
A:LEU84
|
3.7
|
0.0
|
1.0
|
HB2
|
A:CYS86
|
3.8
|
0.0
|
1.0
|
SG
|
A:CYS45
|
4.1
|
0.0
|
1.0
|
H
|
A:CYS48
|
4.2
|
0.0
|
1.0
|
SG
|
A:CYS39
|
4.2
|
0.0
|
1.0
|
CD2
|
A:LEU84
|
4.2
|
0.0
|
1.0
|
HA2
|
A:GLY41
|
4.2
|
0.0
|
1.0
|
H
|
A:CYS86
|
4.3
|
0.0
|
1.0
|
H
|
A:GLY41
|
4.3
|
0.0
|
1.0
|
OE1
|
A:GLU38
|
4.4
|
0.0
|
1.0
|
CA
|
A:CYS86
|
4.5
|
0.0
|
1.0
|
O
|
A:CYS45
|
4.6
|
0.0
|
1.0
|
CB
|
A:LEU84
|
4.6
|
0.0
|
1.0
|
CA
|
A:CYS48
|
4.6
|
0.0
|
1.0
|
HG23
|
A:VAL36
|
4.7
|
0.0
|
1.0
|
H
|
A:GLN87
|
4.7
|
0.0
|
1.0
|
N
|
A:CYS86
|
4.8
|
0.0
|
1.0
|
N
|
A:CYS48
|
4.8
|
0.0
|
1.0
|
HG
|
A:LEU84
|
4.8
|
0.0
|
1.0
|
CG
|
A:LEU84
|
4.8
|
0.0
|
1.0
|
HA
|
A:LEU84
|
4.9
|
0.0
|
1.0
|
HA
|
A:ALA46
|
4.9
|
0.0
|
1.0
|
HB2
|
A:GLU38
|
4.9
|
0.0
|
1.0
|
|
Reference:
H.Mo,
S.S.Pochapsky,
T.C.Pochapsky.
A Model For the Solution Structure of Oxidized Terpredoxin, A FE2S2 Ferredoxin From Pseudomonas. Biochemistry V. 38 5666 1999.
ISSN: ISSN 0006-2960
PubMed: 10220356
DOI: 10.1021/BI983063R
Page generated: Sat Aug 3 02:40:43 2024
|