Iron in PDB 2isa: Crystal Structure of Vibrio Salmonicida Catalase
Enzymatic activity of Crystal Structure of Vibrio Salmonicida Catalase
All present enzymatic activity of Crystal Structure of Vibrio Salmonicida Catalase:
1.11.1.6;
Protein crystallography data
The structure of Crystal Structure of Vibrio Salmonicida Catalase, PDB code: 2isa
was solved by
E.K.Riise,
M.S.Lorentzen,
R.Helland,
A.O.Smalas,
H.K.S.Leiros,
N.P.Willassen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
20.00 /
1.97
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
98.150,
217.760,
99.280,
90.00,
110.48,
90.00
|
|
R / Rfree (%)
|
14.8 /
20
|
Other elements in 2isa:
The structure of Crystal Structure of Vibrio Salmonicida Catalase also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Vibrio Salmonicida Catalase
(pdb code 2isa). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the
Crystal Structure of Vibrio Salmonicida Catalase, PDB code: 2isa:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Iron binding site 1 out
of 8 in 2isa
Go back to
Iron Binding Sites List in 2isa
Iron binding site 1 out
of 8 in the Crystal Structure of Vibrio Salmonicida Catalase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe486
b:8.9
occ:1.00
|
FE
|
A:HEM486
|
0.0
|
8.9
|
1.0
|
|
OH
|
A:TYR337
|
2.0
|
7.5
|
1.0
|
|
NC
|
A:HEM486
|
2.0
|
8.4
|
1.0
|
|
NA
|
A:HEM486
|
2.1
|
7.9
|
1.0
|
|
ND
|
A:HEM486
|
2.1
|
7.4
|
1.0
|
|
NB
|
A:HEM486
|
2.1
|
7.9
|
1.0
|
|
C1A
|
A:HEM486
|
3.0
|
8.3
|
1.0
|
|
C4C
|
A:HEM486
|
3.0
|
8.2
|
1.0
|
|
CZ
|
A:TYR337
|
3.0
|
6.3
|
1.0
|
|
C1C
|
A:HEM486
|
3.1
|
7.9
|
1.0
|
|
C1D
|
A:HEM486
|
3.1
|
7.4
|
1.0
|
|
C4D
|
A:HEM486
|
3.1
|
9.4
|
1.0
|
|
C4B
|
A:HEM486
|
3.1
|
8.8
|
1.0
|
|
C4A
|
A:HEM486
|
3.1
|
7.5
|
1.0
|
|
C1B
|
A:HEM486
|
3.1
|
7.9
|
1.0
|
|
CHA
|
A:HEM486
|
3.4
|
8.4
|
1.0
|
|
CHD
|
A:HEM486
|
3.4
|
7.3
|
1.0
|
|
CHC
|
A:HEM486
|
3.4
|
9.1
|
1.0
|
|
CHB
|
A:HEM486
|
3.5
|
8.3
|
1.0
|
|
CE2
|
A:TYR337
|
3.8
|
5.5
|
1.0
|
|
O
|
A:HOH5671
|
3.8
|
22.8
|
1.0
|
|
CE1
|
A:TYR337
|
3.9
|
5.0
|
1.0
|
|
NE
|
A:ARG333
|
4.1
|
5.9
|
1.0
|
|
NH2
|
A:ARG333
|
4.2
|
3.6
|
1.0
|
|
C3C
|
A:HEM486
|
4.3
|
8.4
|
1.0
|
|
C2A
|
A:HEM486
|
4.3
|
6.4
|
1.0
|
|
C2C
|
A:HEM486
|
4.3
|
10.0
|
1.0
|
|
C2D
|
A:HEM486
|
4.3
|
8.4
|
1.0
|
|
C3A
|
A:HEM486
|
4.3
|
9.2
|
1.0
|
|
C3D
|
A:HEM486
|
4.3
|
7.6
|
1.0
|
|
C3B
|
A:HEM486
|
4.3
|
8.6
|
1.0
|
|
C2B
|
A:HEM486
|
4.3
|
8.5
|
1.0
|
|
CZ
|
A:PHE140
|
4.5
|
9.6
|
1.0
|
|
CZ
|
A:ARG333
|
4.6
|
6.1
|
1.0
|
|
NE2
|
A:HIS54
|
4.7
|
6.3
|
1.0
|
|
CD2
|
A:HIS54
|
4.7
|
7.2
|
1.0
|
|
CE1
|
A:PHE140
|
4.9
|
9.1
|
1.0
|
|
Iron binding site 2 out
of 8 in 2isa
Go back to
Iron Binding Sites List in 2isa
Iron binding site 2 out
of 8 in the Crystal Structure of Vibrio Salmonicida Catalase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe486
b:10.8
occ:1.00
|
FE
|
B:HEM486
|
0.0
|
10.8
|
1.0
|
|
OH
|
B:TYR337
|
1.8
|
6.3
|
1.0
|
|
NB
|
B:HEM486
|
2.1
|
8.7
|
1.0
|
|
ND
|
B:HEM486
|
2.1
|
7.8
|
1.0
|
|
NA
|
B:HEM486
|
2.1
|
8.3
|
1.0
|
|
NC
|
B:HEM486
|
2.1
|
8.0
|
1.0
|
|
CZ
|
B:TYR337
|
2.9
|
7.8
|
1.0
|
|
C4D
|
B:HEM486
|
3.1
|
7.1
|
1.0
|
|
C4C
|
B:HEM486
|
3.1
|
8.0
|
1.0
|
|
C1D
|
B:HEM486
|
3.1
|
8.2
|
1.0
|
|
C1B
|
B:HEM486
|
3.1
|
9.0
|
1.0
|
|
C1A
|
B:HEM486
|
3.1
|
8.1
|
1.0
|
|
C4B
|
B:HEM486
|
3.1
|
8.3
|
1.0
|
|
C4A
|
B:HEM486
|
3.1
|
7.6
|
1.0
|
|
C1C
|
B:HEM486
|
3.1
|
8.4
|
1.0
|
|
CHA
|
B:HEM486
|
3.4
|
7.1
|
1.0
|
|
CHD
|
B:HEM486
|
3.4
|
6.9
|
1.0
|
|
CHB
|
B:HEM486
|
3.5
|
7.6
|
1.0
|
|
CHC
|
B:HEM486
|
3.5
|
7.4
|
1.0
|
|
CE2
|
B:TYR337
|
3.7
|
8.4
|
1.0
|
|
CE1
|
B:TYR337
|
3.8
|
8.1
|
1.0
|
|
O
|
B:HOH6594
|
4.1
|
18.1
|
1.0
|
|
NH2
|
B:ARG333
|
4.1
|
6.0
|
1.0
|
|
NE
|
B:ARG333
|
4.2
|
7.0
|
1.0
|
|
C2B
|
B:HEM486
|
4.3
|
8.5
|
1.0
|
|
C3B
|
B:HEM486
|
4.3
|
8.0
|
1.0
|
|
C3D
|
B:HEM486
|
4.3
|
6.9
|
1.0
|
|
C3C
|
B:HEM486
|
4.3
|
7.0
|
1.0
|
|
C2D
|
B:HEM486
|
4.3
|
6.7
|
1.0
|
|
C2A
|
B:HEM486
|
4.3
|
8.2
|
1.0
|
|
C2C
|
B:HEM486
|
4.3
|
7.7
|
1.0
|
|
C3A
|
B:HEM486
|
4.3
|
8.2
|
1.0
|
|
CZ
|
B:PHE140
|
4.4
|
8.7
|
1.0
|
|
NE2
|
B:HIS54
|
4.6
|
6.1
|
1.0
|
|
CZ
|
B:ARG333
|
4.6
|
7.2
|
1.0
|
|
CD2
|
B:HIS54
|
4.7
|
7.1
|
1.0
|
|
CE1
|
B:PHE140
|
4.8
|
10.1
|
1.0
|
|
CD2
|
B:TYR337
|
5.0
|
7.1
|
1.0
|
|
Iron binding site 3 out
of 8 in 2isa
Go back to
Iron Binding Sites List in 2isa
Iron binding site 3 out
of 8 in the Crystal Structure of Vibrio Salmonicida Catalase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe485
b:10.2
occ:1.00
|
FE
|
C:HEM485
|
0.0
|
10.2
|
1.0
|
|
OH
|
C:TYR337
|
1.8
|
7.5
|
1.0
|
|
NC
|
C:HEM485
|
2.0
|
7.9
|
1.0
|
|
NA
|
C:HEM485
|
2.1
|
7.9
|
1.0
|
|
NB
|
C:HEM485
|
2.1
|
8.8
|
1.0
|
|
ND
|
C:HEM485
|
2.1
|
6.0
|
1.0
|
|
CZ
|
C:TYR337
|
3.0
|
7.6
|
1.0
|
|
C1A
|
C:HEM485
|
3.0
|
7.2
|
1.0
|
|
C4C
|
C:HEM485
|
3.1
|
7.0
|
1.0
|
|
C1C
|
C:HEM485
|
3.1
|
9.0
|
1.0
|
|
C4B
|
C:HEM485
|
3.1
|
8.9
|
1.0
|
|
C4D
|
C:HEM485
|
3.1
|
6.7
|
1.0
|
|
C4A
|
C:HEM485
|
3.1
|
8.2
|
1.0
|
|
C1B
|
C:HEM485
|
3.1
|
9.7
|
1.0
|
|
C1D
|
C:HEM485
|
3.1
|
6.0
|
1.0
|
|
CHA
|
C:HEM485
|
3.4
|
6.1
|
1.0
|
|
CHC
|
C:HEM485
|
3.4
|
8.2
|
1.0
|
|
CHD
|
C:HEM485
|
3.5
|
6.8
|
1.0
|
|
CHB
|
C:HEM485
|
3.5
|
7.8
|
1.0
|
|
CE2
|
C:TYR337
|
3.8
|
7.8
|
1.0
|
|
CE1
|
C:TYR337
|
3.9
|
6.9
|
1.0
|
|
O
|
C:HOH5626
|
4.1
|
25.3
|
1.0
|
|
NH2
|
C:ARG333
|
4.2
|
8.9
|
1.0
|
|
NE
|
C:ARG333
|
4.2
|
7.5
|
1.0
|
|
C2A
|
C:HEM485
|
4.3
|
7.1
|
1.0
|
|
C3C
|
C:HEM485
|
4.3
|
7.7
|
1.0
|
|
C2C
|
C:HEM485
|
4.3
|
7.3
|
1.0
|
|
C3A
|
C:HEM485
|
4.3
|
7.6
|
1.0
|
|
C3B
|
C:HEM485
|
4.3
|
9.4
|
1.0
|
|
C2B
|
C:HEM485
|
4.3
|
9.5
|
1.0
|
|
C3D
|
C:HEM485
|
4.3
|
4.9
|
1.0
|
|
CZ
|
C:PHE140
|
4.3
|
7.0
|
1.0
|
|
C2D
|
C:HEM485
|
4.4
|
5.4
|
1.0
|
|
CZ
|
C:ARG333
|
4.6
|
10.2
|
1.0
|
|
NE2
|
C:HIS54
|
4.6
|
2.0
|
1.0
|
|
CD2
|
C:HIS54
|
4.7
|
4.0
|
1.0
|
|
CE1
|
C:PHE140
|
4.8
|
7.6
|
1.0
|
|
Iron binding site 4 out
of 8 in 2isa
Go back to
Iron Binding Sites List in 2isa
Iron binding site 4 out
of 8 in the Crystal Structure of Vibrio Salmonicida Catalase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe485
b:12.3
occ:1.00
|
FE
|
D:HEM485
|
0.0
|
12.3
|
1.0
|
|
OH
|
D:TYR337
|
1.9
|
7.8
|
1.0
|
|
NB
|
D:HEM485
|
2.1
|
11.8
|
1.0
|
|
NC
|
D:HEM485
|
2.1
|
10.5
|
1.0
|
|
NA
|
D:HEM485
|
2.1
|
10.9
|
1.0
|
|
ND
|
D:HEM485
|
2.1
|
10.5
|
1.0
|
|
CZ
|
D:TYR337
|
3.0
|
7.7
|
1.0
|
|
C1B
|
D:HEM485
|
3.0
|
11.6
|
1.0
|
|
C4C
|
D:HEM485
|
3.1
|
10.2
|
1.0
|
|
C4B
|
D:HEM485
|
3.1
|
11.9
|
1.0
|
|
C4A
|
D:HEM485
|
3.1
|
10.9
|
1.0
|
|
C1C
|
D:HEM485
|
3.1
|
10.5
|
1.0
|
|
C1D
|
D:HEM485
|
3.1
|
10.7
|
1.0
|
|
C1A
|
D:HEM485
|
3.1
|
9.8
|
1.0
|
|
C4D
|
D:HEM485
|
3.1
|
11.6
|
1.0
|
|
CHB
|
D:HEM485
|
3.4
|
10.4
|
1.0
|
|
CHD
|
D:HEM485
|
3.4
|
10.1
|
1.0
|
|
CHC
|
D:HEM485
|
3.5
|
10.9
|
1.0
|
|
CHA
|
D:HEM485
|
3.5
|
10.4
|
1.0
|
|
CE2
|
D:TYR337
|
3.8
|
8.1
|
1.0
|
|
CE1
|
D:TYR337
|
3.9
|
8.4
|
1.0
|
|
NE
|
D:ARG333
|
4.1
|
6.3
|
1.0
|
|
NH2
|
D:ARG333
|
4.2
|
7.2
|
1.0
|
|
C2B
|
D:HEM485
|
4.2
|
11.3
|
1.0
|
|
O
|
D:HOH5669
|
4.2
|
24.8
|
1.0
|
|
C3B
|
D:HEM485
|
4.3
|
11.0
|
1.0
|
|
C3C
|
D:HEM485
|
4.3
|
10.3
|
1.0
|
|
C2C
|
D:HEM485
|
4.3
|
10.3
|
1.0
|
|
C3A
|
D:HEM485
|
4.3
|
9.4
|
1.0
|
|
C2A
|
D:HEM485
|
4.3
|
9.3
|
1.0
|
|
CZ
|
D:PHE140
|
4.3
|
10.9
|
1.0
|
|
C2D
|
D:HEM485
|
4.3
|
10.5
|
1.0
|
|
C3D
|
D:HEM485
|
4.4
|
9.6
|
1.0
|
|
CZ
|
D:ARG333
|
4.6
|
7.0
|
1.0
|
|
NE2
|
D:HIS54
|
4.6
|
7.9
|
1.0
|
|
CD2
|
D:HIS54
|
4.7
|
8.7
|
1.0
|
|
CE1
|
D:PHE140
|
4.8
|
11.2
|
1.0
|
|
Iron binding site 5 out
of 8 in 2isa
Go back to
Iron Binding Sites List in 2isa
Iron binding site 5 out
of 8 in the Crystal Structure of Vibrio Salmonicida Catalase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe486
b:12.7
occ:1.00
|
FE
|
E:HEM486
|
0.0
|
12.7
|
1.0
|
|
OH
|
E:TYR337
|
1.8
|
10.7
|
1.0
|
|
NA
|
E:HEM486
|
2.1
|
10.2
|
1.0
|
|
ND
|
E:HEM486
|
2.1
|
10.9
|
1.0
|
|
NC
|
E:HEM486
|
2.1
|
11.6
|
1.0
|
|
NB
|
E:HEM486
|
2.1
|
12.0
|
1.0
|
|
CZ
|
E:TYR337
|
2.9
|
10.2
|
1.0
|
|
C1A
|
E:HEM486
|
3.0
|
10.5
|
1.0
|
|
C4D
|
E:HEM486
|
3.0
|
10.4
|
1.0
|
|
C4C
|
E:HEM486
|
3.1
|
11.3
|
1.0
|
|
C1D
|
E:HEM486
|
3.1
|
10.7
|
1.0
|
|
C4A
|
E:HEM486
|
3.1
|
10.0
|
1.0
|
|
C1B
|
E:HEM486
|
3.1
|
11.3
|
1.0
|
|
C4B
|
E:HEM486
|
3.1
|
11.6
|
1.0
|
|
C1C
|
E:HEM486
|
3.1
|
12.0
|
1.0
|
|
O
|
E:HOH5919
|
3.2
|
34.2
|
1.0
|
|
CHA
|
E:HEM486
|
3.4
|
9.6
|
1.0
|
|
CHD
|
E:HEM486
|
3.4
|
10.3
|
1.0
|
|
CHC
|
E:HEM486
|
3.5
|
11.8
|
1.0
|
|
CHB
|
E:HEM486
|
3.5
|
10.8
|
1.0
|
|
CE2
|
E:TYR337
|
3.6
|
10.8
|
1.0
|
|
CE1
|
E:TYR337
|
3.9
|
11.1
|
1.0
|
|
NE
|
E:ARG333
|
4.1
|
9.8
|
1.0
|
|
NH2
|
E:ARG333
|
4.1
|
9.4
|
1.0
|
|
C2A
|
E:HEM486
|
4.3
|
10.8
|
1.0
|
|
C3D
|
E:HEM486
|
4.3
|
10.1
|
1.0
|
|
C3C
|
E:HEM486
|
4.3
|
11.6
|
1.0
|
|
C3A
|
E:HEM486
|
4.3
|
11.6
|
1.0
|
|
C3B
|
E:HEM486
|
4.3
|
11.5
|
1.0
|
|
C2B
|
E:HEM486
|
4.3
|
12.0
|
1.0
|
|
C2C
|
E:HEM486
|
4.3
|
11.7
|
1.0
|
|
C2D
|
E:HEM486
|
4.3
|
8.9
|
1.0
|
|
CZ
|
E:PHE140
|
4.4
|
11.8
|
1.0
|
|
O
|
E:HOH5718
|
4.5
|
21.9
|
1.0
|
|
CZ
|
E:ARG333
|
4.5
|
10.6
|
1.0
|
|
CD2
|
E:HIS54
|
4.7
|
11.1
|
1.0
|
|
NE2
|
E:HIS54
|
4.7
|
11.0
|
1.0
|
|
CE1
|
E:PHE140
|
4.8
|
13.4
|
1.0
|
|
CD2
|
E:TYR337
|
4.9
|
9.6
|
1.0
|
|
Iron binding site 6 out
of 8 in 2isa
Go back to
Iron Binding Sites List in 2isa
Iron binding site 6 out
of 8 in the Crystal Structure of Vibrio Salmonicida Catalase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe486
b:12.6
occ:1.00
|
FE
|
F:HEM486
|
0.0
|
12.6
|
1.0
|
|
OH
|
F:TYR337
|
1.8
|
10.7
|
1.0
|
|
ND
|
F:HEM486
|
2.0
|
10.8
|
1.0
|
|
NA
|
F:HEM486
|
2.1
|
11.5
|
1.0
|
|
NC
|
F:HEM486
|
2.1
|
11.4
|
1.0
|
|
NB
|
F:HEM486
|
2.1
|
11.8
|
1.0
|
|
CZ
|
F:TYR337
|
3.0
|
10.2
|
1.0
|
|
C1D
|
F:HEM486
|
3.0
|
11.4
|
1.0
|
|
C4D
|
F:HEM486
|
3.0
|
11.5
|
1.0
|
|
C4C
|
F:HEM486
|
3.1
|
11.5
|
1.0
|
|
C4A
|
F:HEM486
|
3.1
|
12.7
|
1.0
|
|
C1A
|
F:HEM486
|
3.1
|
11.0
|
1.0
|
|
C1B
|
F:HEM486
|
3.1
|
13.2
|
1.0
|
|
C4B
|
F:HEM486
|
3.2
|
12.7
|
1.0
|
|
C1C
|
F:HEM486
|
3.2
|
11.6
|
1.0
|
|
CHD
|
F:HEM486
|
3.4
|
11.3
|
1.0
|
|
CHB
|
F:HEM486
|
3.4
|
12.2
|
1.0
|
|
CHA
|
F:HEM486
|
3.4
|
11.2
|
1.0
|
|
CHC
|
F:HEM486
|
3.6
|
12.1
|
1.0
|
|
CE2
|
F:TYR337
|
3.8
|
11.2
|
1.0
|
|
CE1
|
F:TYR337
|
3.8
|
10.1
|
1.0
|
|
O
|
F:HOH8597
|
4.0
|
28.4
|
1.0
|
|
NE
|
F:ARG333
|
4.2
|
9.3
|
1.0
|
|
C2D
|
F:HEM486
|
4.2
|
9.8
|
1.0
|
|
C3D
|
F:HEM486
|
4.3
|
10.1
|
1.0
|
|
NH2
|
F:ARG333
|
4.3
|
10.9
|
1.0
|
|
C2A
|
F:HEM486
|
4.3
|
12.5
|
1.0
|
|
C3A
|
F:HEM486
|
4.3
|
13.1
|
1.0
|
|
C3C
|
F:HEM486
|
4.3
|
11.2
|
1.0
|
|
C2B
|
F:HEM486
|
4.3
|
13.5
|
1.0
|
|
C3B
|
F:HEM486
|
4.3
|
12.7
|
1.0
|
|
C2C
|
F:HEM486
|
4.4
|
12.3
|
1.0
|
|
CZ
|
F:PHE140
|
4.4
|
11.6
|
1.0
|
|
NE2
|
F:HIS54
|
4.7
|
9.3
|
1.0
|
|
CZ
|
F:ARG333
|
4.7
|
11.6
|
1.0
|
|
CD2
|
F:HIS54
|
4.7
|
10.7
|
1.0
|
|
CE1
|
F:PHE140
|
4.8
|
11.8
|
1.0
|
|
Iron binding site 7 out
of 8 in 2isa
Go back to
Iron Binding Sites List in 2isa
Iron binding site 7 out
of 8 in the Crystal Structure of Vibrio Salmonicida Catalase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Fe485
b:11.6
occ:1.00
|
FE
|
G:HEM485
|
0.0
|
11.6
|
1.0
|
|
OH
|
G:TYR337
|
1.9
|
9.6
|
1.0
|
|
NA
|
G:HEM485
|
2.0
|
9.9
|
1.0
|
|
ND
|
G:HEM485
|
2.1
|
12.2
|
1.0
|
|
NC
|
G:HEM485
|
2.1
|
11.8
|
1.0
|
|
NB
|
G:HEM485
|
2.1
|
11.4
|
1.0
|
|
CZ
|
G:TYR337
|
2.9
|
8.8
|
1.0
|
|
C4C
|
G:HEM485
|
3.0
|
12.0
|
1.0
|
|
C1D
|
G:HEM485
|
3.0
|
10.9
|
1.0
|
|
C1A
|
G:HEM485
|
3.1
|
9.7
|
1.0
|
|
C4A
|
G:HEM485
|
3.1
|
11.2
|
1.0
|
|
C4D
|
G:HEM485
|
3.1
|
10.6
|
1.0
|
|
C1B
|
G:HEM485
|
3.1
|
11.6
|
1.0
|
|
C1C
|
G:HEM485
|
3.1
|
11.4
|
1.0
|
|
C4B
|
G:HEM485
|
3.2
|
12.4
|
1.0
|
|
CHD
|
G:HEM485
|
3.4
|
11.5
|
1.0
|
|
CHA
|
G:HEM485
|
3.4
|
10.2
|
1.0
|
|
CHB
|
G:HEM485
|
3.4
|
10.9
|
1.0
|
|
CHC
|
G:HEM485
|
3.5
|
11.7
|
1.0
|
|
CE2
|
G:TYR337
|
3.7
|
8.2
|
1.0
|
|
CE1
|
G:TYR337
|
3.8
|
7.9
|
1.0
|
|
NE
|
G:ARG333
|
4.2
|
8.8
|
1.0
|
|
O
|
G:HOH5654
|
4.2
|
19.2
|
1.0
|
|
NH2
|
G:ARG333
|
4.2
|
9.6
|
1.0
|
|
C2A
|
G:HEM485
|
4.3
|
9.7
|
1.0
|
|
C3A
|
G:HEM485
|
4.3
|
10.1
|
1.0
|
|
C3C
|
G:HEM485
|
4.3
|
11.5
|
1.0
|
|
C2D
|
G:HEM485
|
4.3
|
11.4
|
1.0
|
|
C3D
|
G:HEM485
|
4.3
|
10.4
|
1.0
|
|
C2B
|
G:HEM485
|
4.3
|
12.0
|
1.0
|
|
C2C
|
G:HEM485
|
4.3
|
11.5
|
1.0
|
|
CZ
|
G:PHE140
|
4.3
|
10.5
|
1.0
|
|
C3B
|
G:HEM485
|
4.4
|
12.3
|
1.0
|
|
NE2
|
G:HIS54
|
4.6
|
8.2
|
1.0
|
|
CZ
|
G:ARG333
|
4.6
|
10.7
|
1.0
|
|
CD2
|
G:HIS54
|
4.6
|
9.2
|
1.0
|
|
CE1
|
G:PHE140
|
4.8
|
12.7
|
1.0
|
|
CD2
|
G:TYR337
|
5.0
|
9.6
|
1.0
|
|
Iron binding site 8 out
of 8 in 2isa
Go back to
Iron Binding Sites List in 2isa
Iron binding site 8 out
of 8 in the Crystal Structure of Vibrio Salmonicida Catalase
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Crystal Structure of Vibrio Salmonicida Catalase within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Fe485
b:12.6
occ:1.00
|
FE
|
H:HEM485
|
0.0
|
12.6
|
1.0
|
|
OH
|
H:TYR337
|
1.9
|
10.0
|
1.0
|
|
NB
|
H:HEM485
|
2.0
|
10.5
|
1.0
|
|
NC
|
H:HEM485
|
2.1
|
11.7
|
1.0
|
|
NA
|
H:HEM485
|
2.1
|
12.2
|
1.0
|
|
ND
|
H:HEM485
|
2.1
|
10.5
|
1.0
|
|
CZ
|
H:TYR337
|
3.0
|
9.8
|
1.0
|
|
C1B
|
H:HEM485
|
3.0
|
11.2
|
1.0
|
|
C4B
|
H:HEM485
|
3.1
|
11.2
|
1.0
|
|
C4A
|
H:HEM485
|
3.1
|
12.5
|
1.0
|
|
C1C
|
H:HEM485
|
3.1
|
11.4
|
1.0
|
|
C4C
|
H:HEM485
|
3.1
|
12.1
|
1.0
|
|
C1D
|
H:HEM485
|
3.1
|
11.2
|
1.0
|
|
C4D
|
H:HEM485
|
3.1
|
10.6
|
1.0
|
|
C1A
|
H:HEM485
|
3.1
|
12.2
|
1.0
|
|
O
|
H:HOH7891
|
3.2
|
25.7
|
1.0
|
|
CHB
|
H:HEM485
|
3.4
|
11.8
|
1.0
|
|
CHC
|
H:HEM485
|
3.4
|
9.8
|
1.0
|
|
CHD
|
H:HEM485
|
3.4
|
10.2
|
1.0
|
|
CHA
|
H:HEM485
|
3.5
|
10.3
|
1.0
|
|
CE2
|
H:TYR337
|
3.7
|
9.5
|
1.0
|
|
CE1
|
H:TYR337
|
3.8
|
10.4
|
1.0
|
|
NE
|
H:ARG333
|
4.0
|
10.0
|
1.0
|
|
NH2
|
H:ARG333
|
4.1
|
6.9
|
1.0
|
|
C2B
|
H:HEM485
|
4.3
|
10.1
|
1.0
|
|
C3B
|
H:HEM485
|
4.3
|
11.0
|
1.0
|
|
C2C
|
H:HEM485
|
4.3
|
10.5
|
1.0
|
|
C3C
|
H:HEM485
|
4.3
|
12.2
|
1.0
|
|
C3A
|
H:HEM485
|
4.3
|
13.2
|
1.0
|
|
C2A
|
H:HEM485
|
4.3
|
11.9
|
1.0
|
|
C3D
|
H:HEM485
|
4.3
|
9.1
|
1.0
|
|
C2D
|
H:HEM485
|
4.3
|
10.5
|
1.0
|
|
CZ
|
H:PHE140
|
4.4
|
11.6
|
1.0
|
|
CZ
|
H:ARG333
|
4.5
|
10.7
|
1.0
|
|
NE2
|
H:HIS54
|
4.6
|
7.3
|
1.0
|
|
O
|
H:HOH7765
|
4.6
|
24.2
|
1.0
|
|
CD2
|
H:HIS54
|
4.6
|
8.5
|
1.0
|
|
CE1
|
H:PHE140
|
4.8
|
13.2
|
1.0
|
|
CD2
|
H:TYR337
|
5.0
|
10.4
|
1.0
|
|
Reference:
E.K.Riise,
M.S.Lorentzen,
R.Helland,
A.O.Smalas,
H.K.S.Leiros,
N.P.Willassen.
The First Structure of A Cold-Active Catalase From Vibrio Salmonicida at 1.96A Reveals Structural Aspects of Cold Adaptation Acta Crystallogr.,Sect.D V. 63 135 2007.
ISSN: ISSN 0907-4449
PubMed: 17242507
DOI: 10.1107/S0907444906043812
Page generated: Sat Aug 3 23:24:28 2024
|
