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Iron in PDB 5x19: Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center

Enzymatic activity of Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center

All present enzymatic activity of Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center:
1.9.3.1;

Protein crystallography data

The structure of Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center, PDB code: 5x19 was solved by A.Shimada, M.Kubo, S.Baba, K.Yamashita, K.Hirata, G.Ueno, T.Nomura, T.Kimura, K.Shinzawa-Itoh, J.Baba, K.Hatano, Y.Eto, A.Miyamoto, H.Murakami, T.Kumasaka, S.Owada, K.Tono, M.Yabashi, Y.Yamaguchi, S.Yanagisawa, M.Sakaguchi, T.Ogura, R.Komiya, J.Yan, E.Yamashita, M.Yamamoto, H.Ago, S.Yoshikawa, T.Tsukihara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 185.034, 208.846, 178.046, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 21

Other elements in 5x19:

The structure of Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Zinc (Zn) 2 atoms
Copper (Cu) 6 atoms
Sodium (Na) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center (pdb code 5x19). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center, PDB code: 5x19:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 5x19

Go back to Iron Binding Sites List in 5x19
Iron binding site 1 out of 4 in the Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe601

b:43.8
occ:1.00
 FE A:HEA601 0.0 43.8 1.0
NE2 A:HIS61 2.0 43.9 1.0
NC A:HEA601 2.0 43.6 1.0
NA A:HEA601 2.1 45.6 1.0
ND A:HEA601 2.1 43.9 1.0
NB A:HEA601 2.1 43.8 1.0
NE2 A:HIS378 2.1 39.3 1.0
CD2 A:HIS61 2.9 40.5 1.0
C4C A:HEA601 3.0 44.0 1.0
CE1 A:HIS61 3.0 43.7 1.0
C4A A:HEA601 3.0 48.0 1.0
CE1 A:HIS378 3.1 43.5 1.0
C1C A:HEA601 3.1 44.3 1.0
CD2 A:HIS378 3.1 39.3 1.0
C4B A:HEA601 3.1 43.5 1.0
C1D A:HEA601 3.1 43.9 1.0
C4D A:HEA601 3.1 43.2 1.0
C1A A:HEA601 3.1 47.1 1.0
C1B A:HEA601 3.1 42.4 1.0
CHD A:HEA601 3.4 41.2 1.0
CHB A:HEA601 3.5 43.8 1.0
CHC A:HEA601 3.5 38.2 1.0
CHA A:HEA601 3.5 44.9 1.0
CG A:HIS61 4.1 43.3 1.0
ND1 A:HIS61 4.2 46.6 1.0
C3C A:HEA601 4.2 42.6 1.0
ND1 A:HIS378 4.2 43.2 1.0
C3A A:HEA601 4.2 42.8 1.0
CG A:HIS378 4.3 38.8 1.0
C2C A:HEA601 4.3 42.3 1.0
C3D A:HEA601 4.3 41.1 1.0
C3B A:HEA601 4.3 40.9 1.0
C2A A:HEA601 4.3 41.7 1.0
C2D A:HEA601 4.3 42.0 1.0
C2B A:HEA601 4.3 43.2 1.0
O A:HOH846 4.7 99.3 1.0
OG A:SER382 4.9 49.0 0.5
CE1 A:PHE377 4.9 41.1 1.0

Iron binding site 2 out of 4 in 5x19

Go back to Iron Binding Sites List in 5x19
Iron binding site 2 out of 4 in the Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe602

b:44.2
occ:1.00
 FE A:HEA602 0.0 44.2 1.0
NC A:HEA602 2.0 45.4 1.0
NA A:HEA602 2.0 43.7 1.0
NB A:HEA602 2.1 38.6 1.0
ND A:HEA602 2.1 43.0 1.0
NE2 A:HIS376 2.2 39.3 1.0
C A:CMO606 2.7 33.9 0.2
C4C A:HEA602 3.0 44.4 1.0
C1C A:HEA602 3.0 46.4 1.0
C1A A:HEA602 3.0 41.6 1.0
C4A A:HEA602 3.0 42.3 1.0
C1B A:HEA602 3.0 42.0 1.0
C4B A:HEA602 3.0 39.4 1.0
C4D A:HEA602 3.1 43.9 1.0
C1D A:HEA602 3.1 44.9 1.0
CD2 A:HIS376 3.2 39.9 1.0
CE1 A:HIS376 3.2 48.5 1.0
O A:CMO606 3.4 35.1 0.2
CHA A:HEA602 3.4 40.0 1.0
CHB A:HEA602 3.4 43.6 1.0
CHC A:HEA602 3.5 41.7 1.0
CHD A:HEA602 3.5 41.6 1.0
C3C A:HEA602 4.2 46.2 1.0
C2C A:HEA602 4.2 46.7 1.0
C3A A:HEA602 4.2 39.5 1.0
C3B A:HEA602 4.3 44.0 1.0
C2A A:HEA602 4.3 41.6 1.0
C2B A:HEA602 4.3 43.1 1.0
C3D A:HEA602 4.3 47.4 1.0
C2D A:HEA602 4.3 46.7 1.0
ND1 A:HIS376 4.4 41.6 1.0
CG A:HIS376 4.4 38.5 1.0

Iron binding site 3 out of 4 in 5x19

Go back to Iron Binding Sites List in 5x19
Iron binding site 3 out of 4 in the Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Fe601

b:53.2
occ:1.00
 FE N:HEA601 0.0 53.2 1.0
NE2 N:HIS378 2.0 53.2 1.0
NE2 N:HIS61 2.0 59.4 1.0
NA N:HEA601 2.1 56.7 1.0
NC N:HEA601 2.1 50.8 1.0
NB N:HEA601 2.1 60.5 1.0
ND N:HEA601 2.1 53.1 1.0
CD2 N:HIS61 2.9 47.5 1.0
CE1 N:HIS378 2.9 49.3 1.0
CD2 N:HIS378 3.0 49.1 1.0
C4A N:HEA601 3.0 54.6 1.0
C4C N:HEA601 3.1 53.0 1.0
C4B N:HEA601 3.1 55.8 1.0
C1D N:HEA601 3.1 54.4 1.0
C1B N:HEA601 3.1 58.2 1.0
C1A N:HEA601 3.1 63.2 1.0
CE1 N:HIS61 3.1 54.6 1.0
C1C N:HEA601 3.1 52.9 1.0
C4D N:HEA601 3.1 55.7 1.0
CHB N:HEA601 3.4 49.9 1.0
CHD N:HEA601 3.4 53.9 1.0
CHA N:HEA601 3.5 58.8 1.0
CHC N:HEA601 3.5 54.5 1.0
ND1 N:HIS378 4.1 53.8 1.0
CG N:HIS61 4.1 56.6 1.0
CG N:HIS378 4.1 51.5 1.0
ND1 N:HIS61 4.2 57.3 1.0
C3A N:HEA601 4.2 54.5 1.0
C2B N:HEA601 4.3 58.6 1.0
C3B N:HEA601 4.3 60.5 1.0
C3C N:HEA601 4.3 49.0 1.0
C2A N:HEA601 4.3 59.9 1.0
C3D N:HEA601 4.3 54.7 1.0
C2D N:HEA601 4.3 55.3 1.0
C2C N:HEA601 4.3 54.2 1.0
CE1 N:PHE377 4.9 48.1 1.0

Iron binding site 4 out of 4 in 5x19

Go back to Iron Binding Sites List in 5x19
Iron binding site 4 out of 4 in the Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Co Bound Cytochrome C Oxidase at 100 Micro Sec After Pump Laser Irradiation to Release Co From O2 Reduction Center within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Fe602

b:50.8
occ:1.00
 FE N:HEA602 0.0 50.8 1.0
NA N:HEA602 2.0 50.1 1.0
NC N:HEA602 2.0 49.0 1.0
NB N:HEA602 2.1 42.6 1.0
ND N:HEA602 2.1 52.8 1.0
NE2 N:HIS376 2.2 52.1 1.0
C N:CMO606 2.8 50.4 0.2
C4A N:HEA602 3.0 45.7 1.0
C4C N:HEA602 3.0 55.8 1.0
C1A N:HEA602 3.0 48.8 1.0
C1C N:HEA602 3.1 52.3 1.0
C1D N:HEA602 3.1 42.8 1.0
C4B N:HEA602 3.1 41.4 1.0
C1B N:HEA602 3.1 44.6 1.0
C4D N:HEA602 3.1 49.6 1.0
CE1 N:HIS376 3.2 49.5 1.0
CD2 N:HIS376 3.2 54.4 1.0
O N:CMO606 3.2 47.0 0.2
CHD N:HEA602 3.4 40.3 1.0
CHB N:HEA602 3.5 43.9 1.0
CHA N:HEA602 3.5 47.8 1.0
CHC N:HEA602 3.5 41.5 1.0
C3A N:HEA602 4.2 46.7 1.0
C2A N:HEA602 4.2 48.1 1.0
C3C N:HEA602 4.2 51.0 1.0
C2C N:HEA602 4.3 51.4 1.0
C2D N:HEA602 4.3 49.8 1.0
C3B N:HEA602 4.3 45.6 1.0
C3D N:HEA602 4.3 49.7 1.0
ND1 N:HIS376 4.3 48.8 1.0
C2B N:HEA602 4.3 45.8 1.0
CG N:HIS376 4.4 47.6 1.0
CG1 N:VAL380 4.9 58.2 1.0
CG2 N:VAL243 4.9 44.6 1.0

Reference:

A.Shimada, M.Kubo, S.Baba, K.Yamashita, K.Hirata, G.Ueno, T.Nomura, T.Kimura, K.Shinzawa-Itoh, J.Baba, K.Hatano, Y.Eto, A.Miyamoto, H.Murakami, T.Kumasaka, S.Owada, K.Tono, M.Yabashi, Y.Yamaguchi, S.Yanagisawa, M.Sakaguchi, T.Ogura, R.Komiya, J.Yan, E.Yamashita, M.Yamamoto, H.Ago, S.Yoshikawa, T.Tsukihara. A Nanosecond Time-Resolved Xfel Analysis of Structural Changes Associated with Co Release From Cytochrome C Oxidase. Sci Adv V. 3 03042 2017.
ISSN: ESSN 2375-2548
PubMed: 28740863
DOI: 10.1126/SCIADV.1603042
Page generated: Tue Aug 6 11:26:26 2024

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