Iron in PDB 6uyk: Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form.
Enzymatic activity of Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form.
All present enzymatic activity of Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form.:
1.3.7.7;
Protein crystallography data
The structure of Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form., PDB code: 6uyk
was solved by
J.P.Bacik,
S.M.S.Imran,
M.B.Watkins,
E.Corless,
E.Antony,
N.Ando,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
41.71 /
2.60
|
Space group
|
I 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
92.513,
100.918,
117.789,
90.00,
99.27,
90.00
|
R / Rfree (%)
|
23.1 /
27.7
|
Other elements in 6uyk:
The structure of Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form. also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form.
(pdb code 6uyk). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the
Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form., PDB code: 6uyk:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Iron binding site 1 out
of 8 in 6uyk
Go back to
Iron Binding Sites List in 6uyk
Iron binding site 1 out
of 8 in the Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe301
b:85.6
occ:1.00
|
FE1
|
A:SF4301
|
0.0
|
85.6
|
1.0
|
S3
|
A:SF4301
|
2.3
|
83.8
|
1.0
|
S4
|
A:SF4301
|
2.3
|
83.8
|
1.0
|
S2
|
A:SF4301
|
2.3
|
83.9
|
1.0
|
SG
|
A:CYS160
|
2.3
|
81.8
|
1.0
|
FE4
|
A:SF4301
|
2.7
|
85.2
|
1.0
|
FE3
|
A:SF4301
|
2.7
|
87.6
|
1.0
|
FE2
|
A:SF4301
|
2.7
|
76.9
|
1.0
|
CB
|
A:CYS160
|
3.4
|
84.0
|
1.0
|
N
|
A:GLY162
|
3.7
|
91.2
|
1.0
|
CA
|
A:GLY162
|
3.8
|
80.8
|
1.0
|
S1
|
A:SF4301
|
3.9
|
85.7
|
1.0
|
CD2
|
A:PHE163
|
4.5
|
77.7
|
1.0
|
N
|
A:PHE163
|
4.5
|
81.9
|
1.0
|
SG
|
A:CYS126
|
4.5
|
84.6
|
1.0
|
SG
|
B:CYS160
|
4.6
|
71.8
|
1.0
|
C
|
A:GLY162
|
4.6
|
88.8
|
1.0
|
CA
|
A:CYS160
|
4.7
|
86.2
|
1.0
|
N
|
A:GLY161
|
4.7
|
90.4
|
1.0
|
C
|
A:CYS160
|
4.7
|
87.6
|
1.0
|
CE2
|
A:PHE163
|
4.7
|
75.9
|
1.0
|
N
|
B:GLY127
|
4.8
|
97.5
|
1.0
|
SG
|
B:CYS126
|
4.9
|
84.7
|
1.0
|
C
|
A:GLY161
|
4.9
|
86.5
|
1.0
|
|
Iron binding site 2 out
of 8 in 6uyk
Go back to
Iron Binding Sites List in 6uyk
Iron binding site 2 out
of 8 in the Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe301
b:76.9
occ:1.00
|
FE2
|
A:SF4301
|
0.0
|
76.9
|
1.0
|
S1
|
A:SF4301
|
2.3
|
85.7
|
1.0
|
S3
|
A:SF4301
|
2.3
|
83.8
|
1.0
|
S4
|
A:SF4301
|
2.3
|
83.8
|
1.0
|
SG
|
B:CYS126
|
2.3
|
84.7
|
1.0
|
FE4
|
A:SF4301
|
2.7
|
85.2
|
1.0
|
FE3
|
A:SF4301
|
2.7
|
87.6
|
1.0
|
FE1
|
A:SF4301
|
2.7
|
85.6
|
1.0
|
CB
|
B:CYS126
|
3.3
|
86.1
|
1.0
|
N
|
B:GLY127
|
3.5
|
97.5
|
1.0
|
CA
|
B:CYS126
|
3.7
|
92.8
|
1.0
|
S2
|
A:SF4301
|
3.9
|
83.9
|
1.0
|
C
|
B:CYS126
|
4.1
|
95.2
|
1.0
|
CA
|
B:GLY162
|
4.1
|
75.0
|
1.0
|
CA
|
B:GLY127
|
4.5
|
89.3
|
1.0
|
N
|
B:GLY162
|
4.6
|
75.6
|
1.0
|
N
|
B:GLY128
|
4.6
|
91.7
|
1.0
|
SG
|
A:CYS126
|
4.7
|
84.6
|
1.0
|
SG
|
A:CYS160
|
4.8
|
81.8
|
1.0
|
SG
|
B:CYS160
|
4.9
|
71.8
|
1.0
|
|
Iron binding site 3 out
of 8 in 6uyk
Go back to
Iron Binding Sites List in 6uyk
Iron binding site 3 out
of 8 in the Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe301
b:87.6
occ:1.00
|
FE3
|
A:SF4301
|
0.0
|
87.6
|
1.0
|
S1
|
A:SF4301
|
2.3
|
85.7
|
1.0
|
S4
|
A:SF4301
|
2.3
|
83.8
|
1.0
|
S2
|
A:SF4301
|
2.3
|
83.9
|
1.0
|
SG
|
A:CYS126
|
2.3
|
84.6
|
1.0
|
FE2
|
A:SF4301
|
2.7
|
76.9
|
1.0
|
FE4
|
A:SF4301
|
2.7
|
85.2
|
1.0
|
FE1
|
A:SF4301
|
2.7
|
85.6
|
1.0
|
CB
|
A:CYS126
|
2.9
|
83.6
|
1.0
|
CA
|
A:CYS126
|
3.1
|
90.0
|
1.0
|
N
|
A:GLY127
|
3.4
|
92.4
|
1.0
|
C
|
A:CYS126
|
3.8
|
92.9
|
1.0
|
S3
|
A:SF4301
|
3.9
|
83.8
|
1.0
|
CA
|
A:GLY162
|
4.1
|
80.8
|
1.0
|
N
|
A:CYS126
|
4.4
|
92.8
|
1.0
|
CA
|
A:GLY127
|
4.6
|
82.7
|
1.0
|
N
|
A:GLY162
|
4.6
|
91.2
|
1.0
|
SG
|
B:CYS126
|
4.7
|
84.7
|
1.0
|
N
|
A:GLY128
|
4.7
|
91.0
|
1.0
|
SG
|
B:CYS160
|
4.8
|
71.8
|
1.0
|
SG
|
A:CYS160
|
4.9
|
81.8
|
1.0
|
CB
|
B:CYS160
|
4.9
|
81.2
|
1.0
|
O
|
A:GLY125
|
5.0
|
95.0
|
1.0
|
O
|
A:CYS126
|
5.0
|
94.8
|
1.0
|
|
Iron binding site 4 out
of 8 in 6uyk
Go back to
Iron Binding Sites List in 6uyk
Iron binding site 4 out
of 8 in the Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe301
b:85.2
occ:1.00
|
FE4
|
A:SF4301
|
0.0
|
85.2
|
1.0
|
S3
|
A:SF4301
|
2.3
|
83.8
|
1.0
|
SG
|
B:CYS160
|
2.3
|
71.8
|
1.0
|
S2
|
A:SF4301
|
2.3
|
83.9
|
1.0
|
S1
|
A:SF4301
|
2.3
|
85.7
|
1.0
|
FE2
|
A:SF4301
|
2.7
|
76.9
|
1.0
|
FE1
|
A:SF4301
|
2.7
|
85.6
|
1.0
|
FE3
|
A:SF4301
|
2.7
|
87.6
|
1.0
|
CB
|
B:CYS160
|
3.2
|
81.2
|
1.0
|
N
|
B:GLY162
|
3.9
|
75.6
|
1.0
|
S4
|
A:SF4301
|
3.9
|
83.8
|
1.0
|
CA
|
B:GLY162
|
4.0
|
75.0
|
1.0
|
CD1
|
B:PHE163
|
4.5
|
78.4
|
1.0
|
CA
|
B:CYS160
|
4.5
|
78.5
|
1.0
|
SG
|
A:CYS160
|
4.6
|
81.8
|
1.0
|
N
|
B:PHE163
|
4.6
|
81.7
|
1.0
|
C
|
B:CYS160
|
4.6
|
81.1
|
1.0
|
CA
|
A:CYS126
|
4.6
|
90.0
|
1.0
|
N
|
A:GLY127
|
4.7
|
92.4
|
1.0
|
SG
|
B:CYS126
|
4.8
|
84.7
|
1.0
|
N
|
B:GLY161
|
4.8
|
80.5
|
1.0
|
C
|
B:GLY162
|
4.8
|
81.0
|
1.0
|
CE1
|
B:PHE163
|
4.9
|
84.5
|
1.0
|
CE2
|
A:PHE163
|
4.9
|
75.9
|
1.0
|
SG
|
A:CYS126
|
5.0
|
84.6
|
1.0
|
|
Iron binding site 5 out
of 8 in 6uyk
Go back to
Iron Binding Sites List in 6uyk
Iron binding site 5 out
of 8 in the Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe301
b:64.7
occ:1.00
|
FE1
|
C:SF4301
|
0.0
|
64.7
|
1.0
|
S2
|
C:SF4301
|
2.3
|
73.6
|
1.0
|
S3
|
C:SF4301
|
2.3
|
65.3
|
1.0
|
S4
|
C:SF4301
|
2.3
|
65.1
|
1.0
|
SG
|
C:CYS160
|
2.3
|
59.8
|
1.0
|
FE4
|
C:SF4301
|
2.7
|
78.8
|
1.0
|
FE2
|
C:SF4301
|
2.7
|
65.9
|
1.0
|
FE3
|
C:SF4301
|
2.7
|
64.8
|
1.0
|
CB
|
C:CYS160
|
3.1
|
61.3
|
1.0
|
N
|
C:GLY162
|
3.5
|
63.1
|
1.0
|
CA
|
C:GLY162
|
3.8
|
61.4
|
1.0
|
S1
|
C:SF4301
|
3.9
|
69.2
|
1.0
|
N
|
C:PHE163
|
4.3
|
60.9
|
1.0
|
N
|
C:GLY161
|
4.4
|
68.8
|
1.0
|
CA
|
C:CYS160
|
4.4
|
66.2
|
1.0
|
C
|
C:CYS160
|
4.5
|
67.6
|
1.0
|
C
|
C:GLY162
|
4.6
|
65.6
|
1.0
|
SG
|
D:CYS160
|
4.6
|
71.8
|
1.0
|
CD2
|
C:PHE163
|
4.6
|
70.0
|
1.0
|
O
|
D:GLY125
|
4.7
|
74.6
|
1.0
|
CE2
|
D:PHE163
|
4.7
|
60.2
|
1.0
|
C
|
C:GLY161
|
4.7
|
71.2
|
1.0
|
CA
|
D:CYS126
|
4.8
|
76.8
|
1.0
|
N
|
D:GLY127
|
4.8
|
70.5
|
1.0
|
SG
|
D:CYS126
|
4.8
|
68.7
|
1.0
|
SG
|
C:CYS126
|
4.8
|
81.9
|
1.0
|
|
Iron binding site 6 out
of 8 in 6uyk
Go back to
Iron Binding Sites List in 6uyk
Iron binding site 6 out
of 8 in the Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe301
b:65.9
occ:1.00
|
FE2
|
C:SF4301
|
0.0
|
65.9
|
1.0
|
S1
|
C:SF4301
|
2.3
|
69.2
|
1.0
|
S4
|
C:SF4301
|
2.3
|
65.1
|
1.0
|
SG
|
D:CYS160
|
2.3
|
71.8
|
1.0
|
S3
|
C:SF4301
|
2.3
|
65.3
|
1.0
|
FE3
|
C:SF4301
|
2.7
|
64.8
|
1.0
|
FE1
|
C:SF4301
|
2.7
|
64.7
|
1.0
|
FE4
|
C:SF4301
|
2.7
|
78.8
|
1.0
|
CB
|
D:CYS160
|
3.0
|
54.2
|
1.0
|
S2
|
C:SF4301
|
3.9
|
73.6
|
1.0
|
N
|
D:GLY162
|
3.9
|
61.6
|
1.0
|
CA
|
D:GLY162
|
4.2
|
60.6
|
1.0
|
CA
|
D:CYS160
|
4.4
|
65.5
|
1.0
|
CD2
|
D:PHE163
|
4.4
|
71.1
|
1.0
|
N
|
D:PHE163
|
4.5
|
65.9
|
1.0
|
SG
|
C:CYS160
|
4.5
|
59.8
|
1.0
|
N
|
D:GLY161
|
4.6
|
62.1
|
1.0
|
C
|
D:CYS160
|
4.6
|
66.0
|
1.0
|
O
|
C:GLY125
|
4.7
|
73.0
|
1.0
|
SG
|
D:CYS126
|
4.7
|
68.7
|
1.0
|
N
|
C:GLY127
|
4.8
|
79.9
|
1.0
|
CE2
|
C:PHE163
|
4.9
|
65.5
|
1.0
|
CE2
|
D:PHE163
|
4.9
|
60.2
|
1.0
|
C
|
D:GLY162
|
4.9
|
69.8
|
1.0
|
SG
|
C:CYS126
|
4.9
|
81.9
|
1.0
|
CA
|
C:CYS126
|
4.9
|
75.0
|
1.0
|
|
Iron binding site 7 out
of 8 in 6uyk
Go back to
Iron Binding Sites List in 6uyk
Iron binding site 7 out
of 8 in the Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe301
b:64.8
occ:1.00
|
FE3
|
C:SF4301
|
0.0
|
64.8
|
1.0
|
S4
|
C:SF4301
|
2.3
|
65.1
|
1.0
|
S1
|
C:SF4301
|
2.3
|
69.2
|
1.0
|
SG
|
D:CYS126
|
2.3
|
68.7
|
1.0
|
S2
|
C:SF4301
|
2.3
|
73.6
|
1.0
|
FE2
|
C:SF4301
|
2.7
|
65.9
|
1.0
|
FE4
|
C:SF4301
|
2.7
|
78.8
|
1.0
|
FE1
|
C:SF4301
|
2.7
|
64.7
|
1.0
|
CB
|
D:CYS126
|
3.3
|
71.2
|
1.0
|
CA
|
D:CYS126
|
3.6
|
76.8
|
1.0
|
N
|
D:GLY127
|
3.7
|
70.5
|
1.0
|
S3
|
C:SF4301
|
3.9
|
65.3
|
1.0
|
CA
|
D:GLY162
|
4.1
|
60.6
|
1.0
|
C
|
D:CYS126
|
4.2
|
75.4
|
1.0
|
N
|
D:GLY162
|
4.4
|
61.6
|
1.0
|
SG
|
C:CYS126
|
4.6
|
81.9
|
1.0
|
O
|
C:GLN19
|
4.6
|
95.7
|
1.0
|
C
|
C:GLN19
|
4.7
|
92.6
|
1.0
|
CG2
|
C:VAL20
|
4.7
|
93.1
|
1.0
|
O
|
D:GLY125
|
4.8
|
74.6
|
1.0
|
CA
|
D:GLY127
|
4.8
|
65.7
|
1.0
|
SG
|
D:CYS160
|
4.8
|
71.8
|
1.0
|
CB
|
C:GLN19
|
4.8
|
88.8
|
1.0
|
N
|
D:GLY128
|
4.8
|
65.5
|
1.0
|
SG
|
C:CYS160
|
4.9
|
59.8
|
1.0
|
N
|
D:CYS126
|
4.9
|
77.2
|
1.0
|
N
|
C:VAL20
|
4.9
|
89.2
|
1.0
|
|
Iron binding site 8 out
of 8 in 6uyk
Go back to
Iron Binding Sites List in 6uyk
Iron binding site 8 out
of 8 in the Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form.
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Dark-Operative Protochlorophyllide Oxidoreductase in the Nucleotide- Free Form. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe301
b:78.8
occ:1.00
|
FE4
|
C:SF4301
|
0.0
|
78.8
|
1.0
|
S2
|
C:SF4301
|
2.3
|
73.6
|
1.0
|
S3
|
C:SF4301
|
2.3
|
65.3
|
1.0
|
S1
|
C:SF4301
|
2.3
|
69.2
|
1.0
|
SG
|
C:CYS126
|
2.3
|
81.9
|
1.0
|
FE1
|
C:SF4301
|
2.7
|
64.7
|
1.0
|
FE3
|
C:SF4301
|
2.7
|
64.8
|
1.0
|
FE2
|
C:SF4301
|
2.7
|
65.9
|
1.0
|
CB
|
C:CYS126
|
3.4
|
80.0
|
1.0
|
N
|
C:GLY127
|
3.5
|
79.9
|
1.0
|
CA
|
C:CYS126
|
3.6
|
75.0
|
1.0
|
CA
|
C:GLY162
|
3.8
|
61.4
|
1.0
|
S4
|
C:SF4301
|
3.9
|
65.1
|
1.0
|
C
|
C:CYS126
|
4.1
|
78.8
|
1.0
|
N
|
C:GLY162
|
4.3
|
63.1
|
1.0
|
O
|
C:GLN19
|
4.4
|
95.7
|
1.0
|
CA
|
C:GLY127
|
4.6
|
72.2
|
1.0
|
CA
|
C:VAL20
|
4.7
|
95.2
|
1.0
|
N
|
C:GLY128
|
4.7
|
76.8
|
1.0
|
SG
|
D:CYS126
|
4.8
|
68.7
|
1.0
|
SG
|
C:CYS160
|
4.8
|
59.8
|
1.0
|
C
|
C:GLY162
|
4.8
|
65.6
|
1.0
|
SG
|
D:CYS160
|
4.9
|
71.8
|
1.0
|
N
|
C:CYS126
|
4.9
|
73.5
|
1.0
|
CB
|
D:CYS160
|
4.9
|
54.2
|
1.0
|
O
|
C:GLY125
|
4.9
|
73.0
|
1.0
|
|
Reference:
E.I.Corless,
S.M.Saad Imran,
M.B.Watkins,
J.P.Bacik,
J.Mattice,
A.Patterson,
K.Danyal,
M.Soffe,
R.Kitelinger,
L.C.Seefeldt,
S.S.Origanti,
B.Bennett,
B.Bothner,
N.Ando,
E.Antony.
The Flexible N-Terminus of Bchl Autoinhibits Activity Through Interaction with Its [4FE-4S] Cluster and Relieved Upon Atp Binding. J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
PubMed: 33219127
DOI: 10.1074/JBC.RA120.016278
Page generated: Wed Aug 7 12:57:13 2024
|