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Iron in PDB 5lc8: Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution

Enzymatic activity of Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution

All present enzymatic activity of Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution:
1.13.11.12; 1.13.11.13;

Protein crystallography data

The structure of Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution, PDB code: 5lc8 was solved by J.Kalms, S.Banthiya, E.Galemou Yoga, H.Kuhn, P.Scheerer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.71 / 1.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 84.332, 97.416, 155.599, 90.00, 90.00, 90.00
R / Rfree (%) 13.9 / 17.1

Other elements in 5lc8:

The structure of Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution (pdb code 5lc8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution, PDB code: 5lc8:

Iron binding site 1 out of 1 in 5lc8

Go back to Iron Binding Sites List in 5lc8
Iron binding site 1 out of 1 in the Crystal Structure of Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution


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 Specific Mutant From Pseudomonas Aeruginosa Lipoxygenase at 1.8A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe701

b:20.3
occ:1.00
 NE2 A:HIS555 2.2 14.7 1.0
O A:ILE685 2.2 17.7 1.0
O A:HOH810 2.2 20.1 1.0
NE2 A:HIS382 2.3 16.9 1.0
NE2 A:HIS377 2.3 17.0 1.0
OD1 A:ASN559 2.4 18.4 1.0
CE1 A:HIS377 3.1 18.1 1.0
CE1 A:HIS555 3.2 16.7 1.0
CD2 A:HIS555 3.2 16.3 1.0
CE1 A:HIS382 3.2 17.6 1.0
C A:ILE685 3.2 22.4 1.0
CG A:ASN559 3.3 18.5 1.0
CD2 A:HIS382 3.3 16.9 1.0
OXT A:ILE685 3.4 22.7 1.0
CD2 A:HIS377 3.4 18.6 1.0
CB A:ASN559 3.8 18.3 1.0
ND1 A:HIS377 4.3 18.7 1.0
ND1 A:HIS555 4.3 18.1 1.0
CG A:HIS555 4.3 17.0 1.0
ND2 A:ASN559 4.3 18.0 1.0
ND1 A:HIS382 4.4 18.3 1.0
CG A:HIS382 4.4 17.4 1.0
CG A:HIS377 4.5 17.5 1.0
CA A:ILE685 4.6 21.2 1.0
CBA A:ZPE703 4.7 31.3 1.0
CG2 A:THR683 4.8 17.8 1.0
CG2 A:ILE685 4.8 22.0 1.0
CA A:ASN559 4.9 17.8 1.0
N A:ILE685 4.9 20.7 1.0

Reference:

J.Kalms, S.Banthiya, E.Galemou Yoga, M.Hamberg, H.G.Holzhutter, H.Kuhn, P.Scheerer. The Crystal Structure of Pseudomonas Aeruginosa Lipoxygenase ALA420GLY Mutant Explains the Improved Oxygen Affinity and the Altered Reaction Specificity. Biochim. Biophys. Acta V.1862 463 2017.
ISSN: ISSN 0006-3002
PubMed: 28093240
DOI: 10.1016/J.BBALIP.2017.01.003
Page generated: Tue Aug 6 04:09:45 2024

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