Iron in PDB 6y9d: Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
Enzymatic activity of Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
All present enzymatic activity of Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine:
1.14.13.239;
Protein crystallography data
The structure of Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine, PDB code: 6y9d
was solved by
M.Quareshy,
M.Shanmugam,
T.D.Bugg,
A.Cameron,
Y.Chen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
81.42 /
1.97
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
91.590,
177.770,
158.800,
90.00,
90.17,
90.00
|
R / Rfree (%)
|
21 /
24.7
|
Iron Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
30;
Page 4, Binding sites: 31 -
36;
Binding sites:
The binding sites of Iron atom in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
(pdb code 6y9d). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 36 binding sites of Iron where determined in the
Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine, PDB code: 6y9d:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 36 in 6y9d
Go back to
Iron Binding Sites List in 6y9d
Iron binding site 1 out
of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe401
b:42.1
occ:1.00
|
NE2
|
A:HIS213
|
2.2
|
42.1
|
1.0
|
O
|
A:HOH535
|
2.3
|
36.3
|
1.0
|
N
|
A:SCN404
|
2.3
|
62.1
|
1.0
|
NE2
|
A:HIS208
|
2.3
|
38.9
|
1.0
|
OD2
|
A:ASP323
|
2.4
|
43.7
|
1.0
|
OD1
|
A:ASP323
|
2.4
|
34.2
|
1.0
|
CG
|
A:ASP323
|
2.7
|
39.3
|
1.0
|
C
|
A:SCN404
|
3.0
|
64.4
|
1.0
|
CE1
|
A:HIS208
|
3.1
|
36.5
|
1.0
|
CE1
|
A:HIS213
|
3.2
|
44.9
|
1.0
|
CD2
|
A:HIS213
|
3.2
|
44.2
|
1.0
|
CD2
|
A:HIS208
|
3.4
|
39.1
|
1.0
|
CB
|
A:ASP323
|
4.2
|
35.3
|
1.0
|
ND1
|
A:HIS213
|
4.2
|
48.8
|
1.0
|
CG
|
A:HIS213
|
4.3
|
49.5
|
1.0
|
ND1
|
A:HIS208
|
4.3
|
35.2
|
1.0
|
O
|
A:HOH588
|
4.3
|
39.6
|
1.0
|
CE1
|
A:PHE319
|
4.4
|
47.2
|
1.0
|
CG
|
A:HIS208
|
4.5
|
36.8
|
1.0
|
OD1
|
A:ASN202
|
4.5
|
37.3
|
1.0
|
S
|
A:SCN404
|
4.5
|
64.9
|
1.0
|
ND2
|
A:ASN202
|
4.6
|
32.0
|
1.0
|
CZ
|
A:PHE319
|
4.6
|
48.0
|
1.0
|
C4
|
A:152403
|
4.7
|
45.9
|
1.0
|
O
|
A:ASN202
|
4.8
|
30.3
|
1.0
|
CG
|
A:ASN202
|
4.9
|
32.3
|
1.0
|
C2
|
A:152403
|
5.0
|
49.0
|
1.0
|
|
Iron binding site 2 out
of 36 in 6y9d
Go back to
Iron Binding Sites List in 6y9d
Iron binding site 2 out
of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe402
b:30.8
occ:1.00
|
FE1
|
A:FES402
|
0.0
|
30.8
|
1.0
|
ND1
|
A:HIS88
|
2.2
|
40.7
|
1.0
|
S2
|
A:FES402
|
2.2
|
49.0
|
1.0
|
S1
|
A:FES402
|
2.2
|
32.1
|
1.0
|
ND1
|
A:HIS109
|
2.2
|
42.0
|
1.0
|
FE2
|
A:FES402
|
3.1
|
35.9
|
1.0
|
CG
|
A:HIS109
|
3.1
|
42.7
|
1.0
|
CE1
|
A:HIS88
|
3.2
|
42.6
|
1.0
|
CG
|
A:HIS88
|
3.2
|
40.7
|
1.0
|
CE1
|
A:HIS109
|
3.3
|
41.3
|
1.0
|
CB
|
A:HIS109
|
3.3
|
42.7
|
1.0
|
CB
|
A:HIS88
|
3.5
|
41.5
|
1.0
|
N
|
A:HIS109
|
3.7
|
41.0
|
1.0
|
CA
|
A:HIS109
|
4.0
|
45.4
|
1.0
|
CB
|
A:TYR108
|
4.1
|
39.2
|
1.0
|
N
|
A:ARG89
|
4.2
|
37.0
|
1.0
|
NE2
|
A:HIS88
|
4.3
|
42.3
|
1.0
|
CD2
|
A:HIS109
|
4.3
|
43.6
|
1.0
|
CD2
|
A:HIS88
|
4.3
|
41.7
|
1.0
|
NE2
|
A:HIS109
|
4.3
|
42.6
|
1.0
|
CG
|
A:TYR108
|
4.4
|
41.1
|
1.0
|
CD2
|
A:TYR108
|
4.5
|
36.6
|
1.0
|
CB
|
A:ARG89
|
4.5
|
41.0
|
1.0
|
C
|
A:TYR108
|
4.5
|
43.6
|
1.0
|
CA
|
A:HIS88
|
4.7
|
40.0
|
1.0
|
SG
|
A:CYS86
|
4.7
|
38.7
|
1.0
|
C
|
A:HIS88
|
4.8
|
40.0
|
1.0
|
SG
|
A:CYS106
|
4.9
|
37.5
|
1.0
|
C
|
A:HIS109
|
4.9
|
48.6
|
1.0
|
CA
|
A:ARG89
|
4.9
|
37.3
|
1.0
|
CA
|
A:TYR108
|
5.0
|
39.9
|
1.0
|
|
Iron binding site 3 out
of 36 in 6y9d
Go back to
Iron Binding Sites List in 6y9d
Iron binding site 3 out
of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe402
b:35.9
occ:1.00
|
FE2
|
A:FES402
|
0.0
|
35.9
|
1.0
|
S2
|
A:FES402
|
2.2
|
49.0
|
1.0
|
S1
|
A:FES402
|
2.2
|
32.1
|
1.0
|
SG
|
A:CYS106
|
2.3
|
37.5
|
1.0
|
SG
|
A:CYS86
|
2.4
|
38.7
|
1.0
|
CB
|
A:CYS86
|
3.0
|
36.0
|
1.0
|
CB
|
A:CYS106
|
3.0
|
38.8
|
1.0
|
FE1
|
A:FES402
|
3.1
|
30.8
|
1.0
|
CB
|
A:TYR108
|
4.2
|
39.2
|
1.0
|
CB
|
A:HIS88
|
4.3
|
41.5
|
1.0
|
N
|
A:HIS109
|
4.3
|
41.0
|
1.0
|
CA
|
A:CYS106
|
4.5
|
39.1
|
1.0
|
CA
|
A:CYS86
|
4.5
|
39.6
|
1.0
|
CB
|
A:HIS91
|
4.5
|
34.0
|
1.0
|
N
|
A:ARG89
|
4.8
|
37.0
|
1.0
|
ND1
|
A:HIS88
|
4.8
|
40.7
|
1.0
|
N
|
A:TYR108
|
4.8
|
43.0
|
1.0
|
CB
|
A:TRP111
|
4.8
|
43.2
|
1.0
|
C
|
A:CYS106
|
4.9
|
39.4
|
1.0
|
N
|
A:HIS91
|
4.9
|
33.0
|
1.0
|
CA
|
A:TYR108
|
5.0
|
39.9
|
1.0
|
|
Iron binding site 4 out
of 36 in 6y9d
Go back to
Iron Binding Sites List in 6y9d
Iron binding site 4 out
of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe401
b:50.2
occ:1.00
|
N
|
B:SCN404
|
2.3
|
82.3
|
1.0
|
O
|
B:HOH562
|
2.3
|
36.7
|
1.0
|
OD1
|
B:ASP323
|
2.4
|
58.2
|
1.0
|
NE2
|
B:HIS213
|
2.4
|
88.8
|
1.0
|
NE2
|
B:HIS208
|
2.5
|
60.3
|
1.0
|
OD2
|
B:ASP323
|
2.5
|
57.0
|
1.0
|
CG
|
B:ASP323
|
2.8
|
54.5
|
1.0
|
C
|
B:SCN404
|
2.9
|
83.8
|
1.0
|
CD2
|
B:HIS213
|
3.3
|
86.7
|
1.0
|
CE1
|
B:HIS213
|
3.3
|
86.0
|
1.0
|
CE1
|
B:HIS208
|
3.4
|
59.3
|
1.0
|
CD2
|
B:HIS208
|
3.5
|
60.8
|
1.0
|
CB
|
B:ASP323
|
4.2
|
47.8
|
1.0
|
CE1
|
B:PHE319
|
4.3
|
60.1
|
1.0
|
ND2
|
B:ASN202
|
4.3
|
40.1
|
1.0
|
S
|
B:SCN404
|
4.4
|
84.6
|
1.0
|
ND1
|
B:HIS213
|
4.4
|
88.5
|
1.0
|
CG
|
B:HIS213
|
4.4
|
87.7
|
1.0
|
ND1
|
B:HIS208
|
4.5
|
59.6
|
1.0
|
OD1
|
B:ASN202
|
4.6
|
45.0
|
1.0
|
CG
|
B:HIS208
|
4.6
|
59.9
|
1.0
|
CZ
|
B:PHE319
|
4.6
|
62.4
|
1.0
|
C4
|
B:152403
|
4.7
|
65.4
|
1.0
|
C2
|
B:152403
|
4.7
|
68.7
|
1.0
|
CG
|
B:ASN202
|
4.8
|
42.6
|
1.0
|
O
|
B:ASN202
|
4.9
|
50.9
|
1.0
|
CA
|
B:ASP323
|
5.0
|
48.2
|
1.0
|
|
Iron binding site 5 out
of 36 in 6y9d
Go back to
Iron Binding Sites List in 6y9d
Iron binding site 5 out
of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe402
b:28.8
occ:1.00
|
FE1
|
B:FES402
|
0.0
|
28.8
|
1.0
|
S1
|
B:FES402
|
2.2
|
28.2
|
1.0
|
S2
|
B:FES402
|
2.2
|
28.4
|
1.0
|
ND1
|
B:HIS88
|
2.2
|
32.8
|
1.0
|
ND1
|
B:HIS109
|
2.3
|
23.7
|
1.0
|
FE2
|
B:FES402
|
2.8
|
35.9
|
1.0
|
CG
|
B:HIS88
|
3.2
|
29.4
|
1.0
|
CG
|
B:HIS109
|
3.2
|
25.8
|
1.0
|
CE1
|
B:HIS88
|
3.2
|
31.9
|
1.0
|
CB
|
B:HIS109
|
3.3
|
27.2
|
1.0
|
CE1
|
B:HIS109
|
3.4
|
24.6
|
1.0
|
CB
|
B:HIS88
|
3.4
|
23.5
|
1.0
|
N
|
B:HIS109
|
3.8
|
31.9
|
1.0
|
CB
|
B:TYR108
|
4.0
|
25.0
|
1.0
|
N
|
B:ARG89
|
4.1
|
23.9
|
1.0
|
CA
|
B:HIS109
|
4.2
|
30.0
|
1.0
|
CD2
|
B:HIS88
|
4.3
|
31.8
|
1.0
|
CG
|
B:TYR108
|
4.3
|
26.7
|
1.0
|
NE2
|
B:HIS88
|
4.3
|
32.3
|
1.0
|
CD2
|
B:TYR108
|
4.3
|
29.1
|
1.0
|
CD2
|
B:HIS109
|
4.4
|
25.6
|
1.0
|
SG
|
B:CYS106
|
4.4
|
24.1
|
1.0
|
NE2
|
B:HIS109
|
4.4
|
25.9
|
1.0
|
CB
|
B:ARG89
|
4.6
|
27.9
|
1.0
|
C
|
B:TYR108
|
4.6
|
31.7
|
1.0
|
SG
|
B:CYS86
|
4.6
|
25.9
|
1.0
|
CA
|
B:HIS88
|
4.7
|
24.0
|
1.0
|
C
|
B:HIS88
|
4.8
|
25.2
|
1.0
|
CA
|
B:ARG89
|
4.9
|
25.7
|
1.0
|
CA
|
B:TYR108
|
4.9
|
27.4
|
1.0
|
C
|
B:HIS109
|
4.9
|
29.4
|
1.0
|
|
Iron binding site 6 out
of 36 in 6y9d
Go back to
Iron Binding Sites List in 6y9d
Iron binding site 6 out
of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe402
b:35.9
occ:1.00
|
FE2
|
B:FES402
|
0.0
|
35.9
|
1.0
|
S2
|
B:FES402
|
2.2
|
28.4
|
1.0
|
S1
|
B:FES402
|
2.2
|
28.2
|
1.0
|
SG
|
B:CYS106
|
2.3
|
24.1
|
1.0
|
SG
|
B:CYS86
|
2.4
|
25.9
|
1.0
|
FE1
|
B:FES402
|
2.8
|
28.8
|
1.0
|
CB
|
B:CYS86
|
3.0
|
24.7
|
1.0
|
CB
|
B:CYS106
|
3.1
|
26.3
|
1.0
|
CB
|
B:HIS88
|
4.0
|
23.5
|
1.0
|
CB
|
B:TYR108
|
4.3
|
25.0
|
1.0
|
CA
|
B:CYS86
|
4.4
|
23.9
|
1.0
|
ND1
|
B:HIS88
|
4.5
|
32.8
|
1.0
|
CB
|
B:HIS91
|
4.6
|
26.9
|
1.0
|
N
|
B:HIS109
|
4.6
|
31.9
|
1.0
|
CA
|
B:CYS106
|
4.6
|
29.0
|
1.0
|
N
|
B:ARG89
|
4.6
|
23.9
|
1.0
|
CG
|
B:HIS88
|
4.7
|
29.4
|
1.0
|
N
|
B:HIS88
|
4.7
|
25.9
|
1.0
|
CA
|
B:HIS88
|
4.9
|
24.0
|
1.0
|
ND1
|
B:HIS109
|
4.9
|
23.7
|
1.0
|
CB
|
B:TRP111
|
4.9
|
23.7
|
1.0
|
C
|
B:CYS86
|
4.9
|
22.7
|
1.0
|
N
|
B:HIS91
|
4.9
|
22.1
|
1.0
|
N
|
B:TYR108
|
5.0
|
24.3
|
1.0
|
|
Iron binding site 7 out
of 36 in 6y9d
Go back to
Iron Binding Sites List in 6y9d
Iron binding site 7 out
of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe401
b:49.1
occ:1.00
|
NE2
|
C:HIS208
|
2.3
|
45.0
|
1.0
|
O
|
C:HOH532
|
2.4
|
42.5
|
1.0
|
OD2
|
C:ASP323
|
2.4
|
47.3
|
1.0
|
N
|
C:SCN404
|
2.4
|
64.9
|
1.0
|
OD1
|
C:ASP323
|
2.4
|
47.3
|
1.0
|
NE2
|
C:HIS213
|
2.5
|
57.5
|
1.0
|
CG
|
C:ASP323
|
2.8
|
45.2
|
1.0
|
CE1
|
C:HIS208
|
3.1
|
43.4
|
1.0
|
CD2
|
C:HIS213
|
3.2
|
59.8
|
1.0
|
C
|
C:SCN404
|
3.3
|
65.8
|
1.0
|
CD2
|
C:HIS208
|
3.4
|
45.6
|
1.0
|
CE1
|
C:HIS213
|
3.5
|
59.9
|
1.0
|
OD1
|
C:ASN202
|
4.3
|
42.2
|
1.0
|
CB
|
C:ASP323
|
4.3
|
42.0
|
1.0
|
ND1
|
C:HIS208
|
4.3
|
44.3
|
1.0
|
ND2
|
C:ASN202
|
4.3
|
41.0
|
1.0
|
CG
|
C:HIS213
|
4.4
|
62.4
|
1.0
|
CG
|
C:HIS208
|
4.5
|
45.1
|
1.0
|
ND1
|
C:HIS213
|
4.5
|
62.5
|
1.0
|
C4
|
C:152403
|
4.5
|
51.2
|
1.0
|
O
|
C:ASN202
|
4.6
|
33.2
|
1.0
|
CG
|
C:ASN202
|
4.7
|
41.4
|
1.0
|
CE1
|
C:PHE319
|
4.8
|
56.8
|
1.0
|
CZ
|
C:PHE319
|
4.8
|
56.3
|
1.0
|
S
|
C:SCN404
|
4.9
|
66.9
|
1.0
|
C2
|
C:152403
|
5.0
|
51.0
|
1.0
|
|
Iron binding site 8 out
of 36 in 6y9d
Go back to
Iron Binding Sites List in 6y9d
Iron binding site 8 out
of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe402
b:41.3
occ:1.00
|
FE1
|
C:FES402
|
0.0
|
41.3
|
1.0
|
S2
|
C:FES402
|
2.2
|
64.7
|
1.0
|
S1
|
C:FES402
|
2.2
|
46.1
|
1.0
|
ND1
|
C:HIS88
|
2.2
|
41.7
|
1.0
|
ND1
|
C:HIS109
|
2.3
|
48.5
|
1.0
|
FE2
|
C:FES402
|
2.9
|
43.3
|
1.0
|
CG
|
C:HIS109
|
3.0
|
50.2
|
1.0
|
CB
|
C:HIS109
|
3.0
|
44.9
|
1.0
|
CE1
|
C:HIS88
|
3.1
|
45.4
|
1.0
|
CG
|
C:HIS88
|
3.3
|
42.3
|
1.0
|
CE1
|
C:HIS109
|
3.4
|
48.2
|
1.0
|
N
|
C:HIS109
|
3.5
|
44.6
|
1.0
|
CB
|
C:HIS88
|
3.7
|
39.5
|
1.0
|
CA
|
C:HIS109
|
3.8
|
47.6
|
1.0
|
CB
|
C:TYR108
|
3.9
|
40.2
|
1.0
|
NE2
|
C:HIS88
|
4.2
|
44.6
|
1.0
|
CG
|
C:TYR108
|
4.3
|
43.3
|
1.0
|
CD2
|
C:HIS109
|
4.3
|
52.1
|
1.0
|
CD2
|
C:HIS88
|
4.4
|
44.1
|
1.0
|
N
|
C:ARG89
|
4.4
|
39.4
|
1.0
|
C
|
C:TYR108
|
4.4
|
46.3
|
1.0
|
CD2
|
C:TYR108
|
4.4
|
43.4
|
1.0
|
SG
|
C:CYS106
|
4.4
|
39.2
|
1.0
|
NE2
|
C:HIS109
|
4.4
|
50.7
|
1.0
|
C
|
C:HIS109
|
4.6
|
48.5
|
1.0
|
CB
|
C:ARG89
|
4.7
|
46.2
|
1.0
|
CA
|
C:TYR108
|
4.7
|
41.3
|
1.0
|
SG
|
C:CYS86
|
4.8
|
44.1
|
1.0
|
CG
|
C:ARG89
|
4.8
|
52.2
|
1.0
|
CA
|
C:HIS88
|
5.0
|
40.2
|
1.0
|
|
Iron binding site 9 out
of 36 in 6y9d
Go back to
Iron Binding Sites List in 6y9d
Iron binding site 9 out
of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe402
b:43.3
occ:1.00
|
FE2
|
C:FES402
|
0.0
|
43.3
|
1.0
|
S2
|
C:FES402
|
2.2
|
64.7
|
1.0
|
S1
|
C:FES402
|
2.2
|
46.1
|
1.0
|
SG
|
C:CYS86
|
2.4
|
44.1
|
1.0
|
SG
|
C:CYS106
|
2.4
|
39.2
|
1.0
|
FE1
|
C:FES402
|
2.9
|
41.3
|
1.0
|
CB
|
C:CYS86
|
3.1
|
42.5
|
1.0
|
CB
|
C:CYS106
|
3.2
|
40.1
|
1.0
|
CB
|
C:HIS88
|
4.0
|
39.5
|
1.0
|
CB
|
C:TYR108
|
4.3
|
40.2
|
1.0
|
ND1
|
C:HIS88
|
4.4
|
41.7
|
1.0
|
N
|
C:HIS109
|
4.5
|
44.6
|
1.0
|
CA
|
C:CYS86
|
4.5
|
39.5
|
1.0
|
CB
|
C:HIS91
|
4.5
|
33.5
|
1.0
|
CA
|
C:CYS106
|
4.6
|
39.1
|
1.0
|
N
|
C:ARG89
|
4.7
|
39.4
|
1.0
|
CG
|
C:HIS88
|
4.7
|
42.3
|
1.0
|
N
|
C:HIS88
|
4.8
|
38.4
|
1.0
|
N
|
C:HIS91
|
4.9
|
32.3
|
1.0
|
CA
|
C:HIS88
|
4.9
|
40.2
|
1.0
|
C
|
C:CYS86
|
5.0
|
38.1
|
1.0
|
N
|
C:TYR108
|
5.0
|
39.8
|
1.0
|
CB
|
C:TRP111
|
5.0
|
44.7
|
1.0
|
|
Iron binding site 10 out
of 36 in 6y9d
Go back to
Iron Binding Sites List in 6y9d
Iron binding site 10 out
of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Substrate L-Carnitine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe401
b:46.1
occ:1.00
|
N
|
D:SCN404
|
2.2
|
69.1
|
1.0
|
NE2
|
D:HIS208
|
2.2
|
39.7
|
1.0
|
NE2
|
D:HIS213
|
2.3
|
47.0
|
1.0
|
OD1
|
D:ASP323
|
2.4
|
33.4
|
1.0
|
O
|
D:HOH540
|
2.4
|
37.8
|
1.0
|
OD2
|
D:ASP323
|
2.6
|
39.5
|
1.0
|
CG
|
D:ASP323
|
2.8
|
35.1
|
1.0
|
C
|
D:SCN404
|
3.0
|
72.8
|
1.0
|
CE1
|
D:HIS208
|
3.1
|
39.1
|
1.0
|
CD2
|
D:HIS213
|
3.2
|
49.8
|
1.0
|
CE1
|
D:HIS213
|
3.2
|
49.6
|
1.0
|
CD2
|
D:HIS208
|
3.3
|
41.1
|
1.0
|
ND1
|
D:HIS208
|
4.3
|
38.9
|
1.0
|
CB
|
D:ASP323
|
4.3
|
31.4
|
1.0
|
ND1
|
D:HIS213
|
4.3
|
53.0
|
1.0
|
CG
|
D:HIS213
|
4.3
|
54.5
|
1.0
|
CG
|
D:HIS208
|
4.4
|
39.5
|
1.0
|
OD1
|
D:ASN202
|
4.4
|
36.8
|
1.0
|
ND2
|
D:ASN202
|
4.5
|
34.5
|
1.0
|
O
|
D:HOH584
|
4.6
|
38.8
|
1.0
|
S
|
D:SCN404
|
4.6
|
74.6
|
1.0
|
CE1
|
D:PHE319
|
4.6
|
46.8
|
1.0
|
C4
|
D:152403
|
4.7
|
50.2
|
1.0
|
O
|
D:ASN202
|
4.8
|
34.0
|
1.0
|
CZ
|
D:PHE319
|
4.8
|
47.4
|
1.0
|
CG
|
D:ASN202
|
4.9
|
34.3
|
1.0
|
C2
|
D:152403
|
4.9
|
53.2
|
1.0
|
|
Reference:
M.Quareshy,
M.Shanmugam,
E.Townsend,
E.Jameson,
T.D.H.Bugg,
A.D.Cameron,
Y.Chen.
Structural Basis of Carnitine Monooxygenase Cnta Substrate Specificity, Inhibition and Inter-Subunit Electron Transfer. J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
PubMed: 33158989
DOI: 10.1074/JBC.RA120.016019
Page generated: Wed Aug 7 15:55:50 2024
|