Atomistry » Iron » PDB 4o1w-4oxf » 4ou9
Atomistry »
  Iron »
    PDB 4o1w-4oxf »
      4ou9 »

Iron in PDB 4ou9: Crystal Structure of Apocarotenoid Oxygenase in the Presence of Triton X-100

Enzymatic activity of Crystal Structure of Apocarotenoid Oxygenase in the Presence of Triton X-100

All present enzymatic activity of Crystal Structure of Apocarotenoid Oxygenase in the Presence of Triton X-100:
1.13.11.75;

Protein crystallography data

The structure of Crystal Structure of Apocarotenoid Oxygenase in the Presence of Triton X-100, PDB code: 4ou9 was solved by X.Sui, K.Palczewski, P.D.Kiser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.61 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 118.470, 125.390, 202.540, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.5

Other elements in 4ou9:

The structure of Crystal Structure of Apocarotenoid Oxygenase in the Presence of Triton X-100 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Apocarotenoid Oxygenase in the Presence of Triton X-100 (pdb code 4ou9). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Apocarotenoid Oxygenase in the Presence of Triton X-100, PDB code: 4ou9:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4ou9

Go back to Iron Binding Sites List in 4ou9
Iron binding site 1 out of 4 in the Crystal Structure of Apocarotenoid Oxygenase in the Presence of Triton X-100


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 Apocarotenoid Oxygenase in the Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:32.7
occ:1.00
 O A:HOH791 2.1 38.3 1.0
NE2 A:HIS304 2.2 33.8 1.0
NE2 A:HIS238 2.2 35.5 1.0
NE2 A:HIS484 2.2 28.9 1.0
NE2 A:HIS183 2.2 30.6 1.0
CE1 A:HIS183 2.9 32.3 1.0
CD2 A:HIS484 3.0 28.4 1.0
CD2 A:HIS238 3.1 36.5 1.0
CD2 A:HIS304 3.1 33.2 1.0
CE1 A:HIS304 3.2 33.1 1.0
CE1 A:HIS238 3.2 36.0 1.0
CE1 A:HIS484 3.3 29.3 1.0
CD2 A:HIS183 3.4 32.3 1.0
CG A:HIS484 4.2 27.9 1.0
ND1 A:HIS183 4.2 34.0 1.0
ND1 A:HIS484 4.3 29.7 1.0
CG A:HIS238 4.3 36.0 1.0
CG A:HIS304 4.3 32.6 1.0
ND1 A:HIS304 4.3 32.4 1.0
ND1 A:HIS238 4.3 36.2 1.0
CG A:HIS183 4.4 31.2 1.0
CG2 A:THR136 4.5 27.8 1.0

Iron binding site 2 out of 4 in 4ou9

Go back to Iron Binding Sites List in 4ou9
Iron binding site 2 out of 4 in the Crystal Structure of Apocarotenoid Oxygenase in the Presence of Triton X-100


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 Apocarotenoid Oxygenase in the Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:32.5
occ:1.00
 O B:HOH781 2.1 39.1 1.0
NE2 B:HIS304 2.1 33.1 1.0
NE2 B:HIS183 2.2 33.9 1.0
NE2 B:HIS484 2.2 31.1 1.0
NE2 B:HIS238 2.2 34.5 1.0
CE1 B:HIS183 2.9 34.1 1.0
CD2 B:HIS484 3.1 29.4 1.0
CD2 B:HIS304 3.1 31.5 1.0
CE1 B:HIS304 3.1 31.5 1.0
CE1 B:HIS484 3.2 29.5 1.0
CD2 B:HIS238 3.2 34.8 1.0
CE1 B:HIS238 3.2 34.9 1.0
CD2 B:HIS183 3.3 32.2 1.0
ND1 B:HIS183 4.2 34.3 1.0
CG B:HIS484 4.2 29.0 1.0
ND1 B:HIS484 4.2 29.5 1.0
ND1 B:HIS304 4.2 33.9 1.0
CG B:HIS304 4.2 33.7 1.0
ND1 B:HIS238 4.3 35.0 1.0
CG B:HIS238 4.3 34.3 1.0
CG B:HIS183 4.4 30.6 1.0
CG2 B:THR136 4.6 27.2 1.0

Iron binding site 3 out of 4 in 4ou9

Go back to Iron Binding Sites List in 4ou9
Iron binding site 3 out of 4 in the Crystal Structure of Apocarotenoid Oxygenase in the Presence of Triton X-100


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 Apocarotenoid Oxygenase in the Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:34.0
occ:0.98
 O C:HOH773 2.2 35.9 1.0
NE2 C:HIS183 2.2 35.5 1.0
NE2 C:HIS304 2.2 33.5 1.0
NE2 C:HIS484 2.2 33.0 1.0
NE2 C:HIS238 2.3 39.4 1.0
CE1 C:HIS183 2.9 35.9 1.0
CE1 C:HIS238 3.1 39.8 1.0
CD2 C:HIS304 3.2 33.6 1.0
CD2 C:HIS484 3.2 32.0 1.0
CE1 C:HIS484 3.2 33.9 1.0
CE1 C:HIS304 3.3 33.0 1.0
CD2 C:HIS238 3.3 37.3 1.0
CD2 C:HIS183 3.3 36.4 1.0
ND1 C:HIS183 4.1 36.5 1.0
ND1 C:HIS484 4.2 32.9 1.0
CG C:HIS484 4.2 32.0 1.0
ND1 C:HIS238 4.3 37.8 1.0
CG C:HIS183 4.3 35.2 1.0
CG C:HIS304 4.3 33.1 1.0
ND1 C:HIS304 4.3 34.1 1.0
CG C:HIS238 4.4 38.8 1.0
CG2 C:THR136 4.6 34.4 1.0

Iron binding site 4 out of 4 in 4ou9

Go back to Iron Binding Sites List in 4ou9
Iron binding site 4 out of 4 in the Crystal Structure of Apocarotenoid Oxygenase in the Presence of Triton X-100


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 Apocarotenoid Oxygenase in the Presence of Triton X-100 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:36.3
occ:1.00
 O D:HOH751 2.0 40.5 1.0
NE2 D:HIS183 2.2 35.2 1.0
NE2 D:HIS304 2.2 32.7 1.0
NE2 D:HIS484 2.2 35.2 1.0
NE2 D:HIS238 2.3 38.0 1.0
CE1 D:HIS183 2.9 39.2 1.0
CD2 D:HIS484 3.1 32.7 1.0
CD2 D:HIS304 3.1 33.3 1.0
CE1 D:HIS304 3.2 33.1 1.0
CE1 D:HIS484 3.2 35.5 1.0
CD2 D:HIS238 3.2 37.3 1.0
CE1 D:HIS238 3.3 38.1 1.0
CD2 D:HIS183 3.3 37.2 1.0
ND1 D:HIS183 4.1 38.4 1.0
CG D:HIS484 4.2 33.8 1.0
ND1 D:HIS484 4.2 34.4 1.0
ND1 D:HIS304 4.3 33.9 1.0
CG D:HIS304 4.3 32.7 1.0
CG D:HIS183 4.3 38.3 1.0
ND1 D:HIS238 4.4 36.6 1.0
CG D:HIS238 4.4 37.6 1.0
CG2 D:THR136 4.6 32.3 1.0

Reference:

X.Sui, P.D.Kiser, T.Che, P.R.Carey, M.Golczak, W.Shi, J.Von Lintig, K.Palczewski. Analysis of Carotenoid Isomerase Activity in A Prototypical Carotenoid Cleavage Enzyme, Apocarotenoid Oxygenase (Aco). J.Biol.Chem. V. 289 12286 2014.
ISSN: ISSN 0021-9258
PubMed: 24648526
DOI: 10.1074/JBC.M114.552836
Page generated: Mon Aug 5 08:14:31 2024

Last articles

F in 4N94
F in 4N98
F in 4N8Q
F in 4N7E
F in 4N5V
F in 4N70
F in 4N5G
F in 4N07
F in 4MUK
F in 4N3R
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy