Iron in PDB 4kvq: Crystal Structure of Prochlorococcus Marinus Aldehyde-Deformylating Oxygenase Wild Type with Palmitic Acid Bound

All present enzymatic activity of Crystal Structure of Prochlorococcus Marinus Aldehyde-Deformylating Oxygenase Wild Type with Palmitic Acid Bound:
4.1.99.5;

The structure of Crystal Structure of Prochlorococcus Marinus Aldehyde-Deformylating Oxygenase Wild Type with Palmitic Acid Bound, PDB code: 4kvq was solved by C.W.Levy, B.Khara, N.Menon, D.Mansell, D.Das, E.N.G.Marsh, D.Leys, N.S.Scrutton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.55 / 1.84
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	77.030, 77.030, 115.860, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 21.7

The binding sites of Iron atom in the Crystal Structure of Prochlorococcus Marinus Aldehyde-Deformylating Oxygenase Wild Type with Palmitic Acid Bound (pdb code 4kvq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Prochlorococcus Marinus Aldehyde-Deformylating Oxygenase Wild Type with Palmitic Acid Bound, PDB code: 4kvq:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Prochlorococcus Marinus Aldehyde-Deformylating Oxygenase Wild Type with Palmitic Acid Bound


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 Prochlorococcus Marinus Aldehyde-Deformylating Oxygenase Wild Type with Palmitic Acid Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:19.0 occ:1.00 OE1 A:GLU73 2.0 26.6 1.0 O1 A:PLM303 2.0 39.4 1.0 OE1 A:GLU45 2.1 23.2 1.0 OE1 A:GLU157 2.2 36.3 1.0 ND1 A:HIS76 2.2 19.3 1.0 OE2 A:GLU157 2.8 35.8 1.0 CD A:GLU157 2.8 43.1 1.0 CD A:GLU45 2.8 23.2 1.0 OE2 A:GLU45 2.9 28.6 1.0 CE1 A:HIS76 3.0 26.2 1.0 C1 A:PLM303 3.1 24.6 1.0 CD A:GLU73 3.1 23.9 1.0 CG A:HIS76 3.3 20.8 1.0 FE A:FE302 3.4 20.0 1.0 C2 A:PLM303 3.4 34.5 1.0 OE2 A:GLU73 3.6 18.6 1.0 CB A:HIS76 3.8 18.7 1.0 NE2 A:HIS76 4.2 22.3 1.0 O2 A:PLM303 4.2 31.6 1.0 CG A:GLU45 4.3 16.0 1.0 CG A:GLU157 4.3 28.6 1.0 CA A:GLU73 4.4 19.7 1.0 CD2 A:HIS76 4.4 20.7 1.0 CG A:GLU73 4.4 18.2 1.0 CE1 A:HIS160 4.6 26.4 1.0 CB A:GLU73 4.6 17.3 1.0 CG1 A:VAL153 4.6 32.2 1.0 ND1 A:HIS160 4.7 19.7 1.0 CB A:GLU45 4.8 18.0 1.0 C3 A:PLM303 4.9 24.8 1.0 OE1 A:GLU128 5.0 19.4 1.0 CA A:GLU45 5.0 19.0 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Prochlorococcus Marinus Aldehyde-Deformylating Oxygenase Wild Type with Palmitic Acid Bound


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 Prochlorococcus Marinus Aldehyde-Deformylating Oxygenase Wild Type with Palmitic Acid Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe302 b:20.0 occ:1.00 OE2 A:GLU73 2.1 18.6 1.0 O1 A:PLM303 2.1 39.4 1.0 OE2 A:GLU157 2.2 35.8 1.0 OE2 A:GLU128 2.2 17.9 1.0 ND1 A:HIS160 2.2 19.7 1.0 OE1 A:GLU128 2.3 19.4 1.0 CD A:GLU128 2.6 17.8 1.0 C1 A:PLM303 2.8 24.6 1.0 CD A:GLU73 2.9 23.9 1.0 O2 A:PLM303 3.0 31.6 1.0 CE1 A:HIS160 3.0 26.4 1.0 OE1 A:GLU73 3.1 26.6 1.0 CD A:GLU157 3.2 43.1 1.0 FE A:FE301 3.4 19.0 1.0 CG A:HIS160 3.4 24.2 1.0 OE1 A:GLU157 3.8 36.3 1.0 CB A:HIS160 3.8 19.6 1.0 CG A:GLU128 4.1 16.0 1.0 NE2 A:HIS160 4.2 25.7 1.0 C2 A:PLM303 4.3 34.5 1.0 CE2 A:TYR52 4.3 20.6 1.0 NE2 A:GLN123 4.3 18.4 1.0 CG A:GLU73 4.4 18.2 1.0 CG A:GLU157 4.4 28.6 1.0 CD2 A:HIS160 4.4 22.7 1.0 OH A:TYR52 4.5 20.0 1.0 CB A:GLU157 4.5 32.4 1.0 CA A:GLU157 4.6 24.0 1.0 CB A:ALA48 4.6 18.5 1.0 CE1 A:HIS76 4.8 26.2 1.0 ND1 A:HIS76 4.8 19.3 1.0 CZ A:TYR52 4.9 20.8 1.0 CB A:GLU128 5.0 17.0 1.0

B.Khara, N.Menon, C.Levy, D.Mansell, D.Das, E.N.Marsh, D.Leys, N.S.Scrutton. Production of Propane and Other Short-Chain Alkanes By Structure-Based Engineering of Ligand Specificity in Aldehyde-Deformylating Oxygenase. Chembiochem V. 14 1204 2013.
ISSN: ISSN 1439-4227
PubMed: 23757044
DOI: 10.1002/CBIC.201300307