Iron in PDB 5kja: Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA

Enzymatic activity of Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA

All present enzymatic activity of Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA:
1.13.11.75;

Protein crystallography data

The structure of Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA, PDB code: 5kja was solved by X.Sui, P.D.Kiser, K.Palczewski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.62 / 2.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 118.140, 125.260, 203.570, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 23.9

Other elements in 5kja:

The structure of Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA (pdb code 5kja). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 5 binding sites of Iron where determined in the Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA, PDB code: 5kja:
Jump to Iron binding site number: 1; 2; 3; 4; 5;

Iron binding site 1 out of 5 in 5kja

Go back to Iron Binding Sites List in 5kja
Iron binding site 1 out of 5 in the Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:96.8
occ:1.00
 NE2 A:HIS304 2.6 60.6 1.0
NE2 A:HIS484 2.8 40.8 1.0
NE2 A:HIS183 3.0 60.0 1.0
CE1 A:HIS183 3.2 53.3 1.0
CE1 A:HIS304 3.3 54.7 1.0
NE2 A:HIS238 3.5 0.3 1.0
CD2 A:HIS484 3.5 43.0 1.0
CD2 A:HIS238 3.8 0.8 1.0
CD2 A:HIS304 3.8 59.4 1.0
CE1 A:HIS484 4.0 44.0 1.0
CD2 A:HIS183 4.4 53.5 1.0
ND1 A:HIS183 4.5 47.3 1.0
OE1 A:GLU150 4.5 91.1 1.0
CG2 A:THR136 4.5 33.0 1.0
CZ A:PHE303 4.5 80.4 1.0
ND1 A:HIS304 4.6 51.3 1.0
CE2 A:PHE303 4.7 79.7 1.0
CE1 A:HIS238 4.7 0.1 1.0
CG A:HIS484 4.8 41.9 1.0
CG A:HIS304 4.8 52.9 1.0
ND1 A:HIS484 5.0 42.8 1.0

Iron binding site 2 out of 5 in 5kja

Go back to Iron Binding Sites List in 5kja
Iron binding site 2 out of 5 in the Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:97.3
occ:1.00
 NE2 B:HIS304 2.5 55.8 1.0
NE2 B:HIS484 2.7 30.7 1.0
NE2 B:HIS183 2.8 51.6 1.0
CE1 B:HIS183 3.0 48.3 1.0
CE1 B:HIS304 3.2 58.9 1.0
CD2 B:HIS484 3.3 32.5 1.0
NE2 B:HIS238 3.6 0.7 1.0
CD2 B:HIS304 3.7 55.8 1.0
CE1 B:HIS484 3.8 32.4 1.0
CD2 B:HIS238 3.8 0.6 1.0
CD2 B:HIS183 4.1 48.0 1.0
ND1 B:HIS183 4.3 43.8 1.0
ND1 B:HIS304 4.5 56.7 1.0
CG2 B:THR136 4.5 37.5 1.0
OE1 B:GLU150 4.5 79.3 1.0
CG B:HIS484 4.6 35.0 1.0
CZ B:PHE303 4.7 75.8 1.0
CG B:HIS304 4.7 58.1 1.0
CE2 B:PHE303 4.7 74.4 1.0
ND1 B:HIS484 4.8 34.1 1.0
CE1 B:HIS238 4.9 0.1 1.0
CG B:HIS183 4.9 43.3 1.0

Iron binding site 3 out of 5 in 5kja

Go back to Iron Binding Sites List in 5kja
Iron binding site 3 out of 5 in the Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:91.5
occ:1.00
 NE2 C:HIS304 2.6 56.0 1.0
NE2 C:HIS484 2.7 42.9 1.0
NE2 C:HIS183 3.1 57.3 1.0
CE1 C:HIS304 3.2 58.5 1.0
CE1 C:HIS183 3.3 54.3 1.0
CD2 C:HIS484 3.4 42.5 1.0
NE2 C:HIS238 3.7 0.3 1.0
CE1 C:HIS484 3.8 47.5 1.0
CD2 C:HIS304 3.9 57.8 1.0
CD2 C:HIS238 4.0 0.5 1.0
CD2 C:HIS183 4.5 54.2 1.0
ND1 C:HIS304 4.5 55.2 1.0
CG2 C:THR136 4.5 38.4 1.0
CZ C:PHE303 4.6 72.0 1.0
ND1 C:HIS183 4.6 58.5 1.0
CG C:HIS484 4.7 45.9 1.0
CE2 C:PHE303 4.7 73.5 1.0
OE1 C:GLU150 4.7 88.9 1.0
CG C:HIS304 4.8 52.8 1.0
ND1 C:HIS484 4.8 48.2 1.0
CE1 C:HIS238 4.9 0.7 1.0
CD2 C:LEU483 4.9 50.9 1.0

Iron binding site 4 out of 5 in 5kja

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Iron binding site 4 out of 5 in the Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:96.9
occ:1.00
 NE2 D:HIS484 2.3 48.9 1.0
NE2 D:HIS304 2.5 56.8 1.0
NE2 D:HIS183 2.8 66.1 1.0
CD2 D:HIS484 3.1 45.4 1.0
CE1 D:HIS304 3.2 53.2 1.0
CE1 D:HIS183 3.2 59.9 1.0
CE1 D:HIS484 3.5 50.5 1.0
CD2 D:HIS304 3.7 54.1 1.0
NE2 D:HIS238 3.9 0.5 1.0
CD2 D:HIS183 4.1 60.2 1.0
CD2 D:HIS238 4.2 0.6 1.0
CG D:HIS484 4.3 44.6 1.0
ND1 D:HIS304 4.4 50.1 1.0
ND1 D:HIS183 4.5 57.5 1.0
ND1 D:HIS484 4.5 49.4 1.0
CG2 D:THR136 4.6 37.9 1.0
CG D:HIS304 4.7 50.5 1.0
OE1 D:GLU150 4.8 1.0 1.0
CE2 D:PHE303 4.9 72.4 1.0
CZ D:PHE303 4.9 76.2 1.0
CE1 D:PHE371 4.9 45.4 1.0
CG D:HIS183 5.0 54.6 1.0

Iron binding site 5 out of 5 in 5kja

Go back to Iron Binding Sites List in 5kja
Iron binding site 5 out of 5 in the Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Synechocystis Apocarotenoid Oxygenase (Aco) Mutant - TRP149ALA within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe501

b:0.1
occ:1.00
 NE2 E:HIS484 3.1 0.0 1.0
NE2 E:HIS304 3.3 0.6 1.0
CD2 E:HIS484 3.6 0.2 1.0
NE2 E:HIS238 3.6 0.6 1.0
NE2 E:HIS183 3.7 0.7 1.0
CE1 E:HIS304 3.7 0.7 1.0
CE1 E:HIS183 3.7 0.3 1.0
CD2 E:HIS238 4.2 0.3 1.0
CG2 E:THR136 4.2 93.2 1.0
CE1 E:HIS484 4.3 0.6 1.0
CD2 E:LEU483 4.3 89.9 1.0
CD2 E:HIS304 4.6 0.0 1.0
CZ E:PHE303 4.6 0.1 1.0
OE1 E:GLU150 4.6 0.2 1.0
CE1 E:HIS238 4.7 0.3 1.0
CE2 E:PHE303 4.8 0.1 1.0
CG E:HIS484 4.9 0.4 1.0

Reference:

X.Sui, J.Zhang, M.Golczak, K.Palczewski, P.D.Kiser. Key Residues For Catalytic Function and Metal Coordination in A Carotenoid Cleavage Dioxygenase. J.Biol.Chem. V. 291 19401 2016.
ISSN: ESSN 1083-351X
PubMed: 27453555
DOI: 10.1074/JBC.M116.744912
Page generated: Tue Aug 6 03:27:15 2024

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