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:

Chlorine (Cl) 2 atoms

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

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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

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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

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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

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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

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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

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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

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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: Sun Dec 13 17:17:18 2020

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