Iron in PDB 5v5r: Dehaloperoxidase A I9L Mutant

The structure of Dehaloperoxidase A I9L Mutant, PDB code: 5v5r was solved by L.M.Carey, R.A.Ghiladi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.58 / 1.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.665, 67.423, 68.910, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 16.9

The binding sites of Iron atom in the Dehaloperoxidase A I9L Mutant (pdb code 5v5r). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Dehaloperoxidase A I9L Mutant, PDB code: 5v5r:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Dehaloperoxidase A I9L Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Dehaloperoxidase A I9L Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:12.3 occ:1.00 FE B:HEM201 0.0 12.3 1.0 NA B:HEM201 2.0 13.5 1.0 ND B:HEM201 2.0 14.2 1.0 NC B:HEM201 2.0 12.8 1.0 NB B:HEM201 2.0 11.8 1.0 NE2 B:HIS89 2.1 13.3 1.0 O1 B:OXY202 2.5 19.1 1.0 C4A B:HEM201 3.0 12.1 1.0 C4C B:HEM201 3.0 13.6 1.0 C1D B:HEM201 3.0 13.9 1.0 C4D B:HEM201 3.1 14.7 1.0 C1C B:HEM201 3.1 12.7 1.0 C4B B:HEM201 3.1 11.5 1.0 C1B B:HEM201 3.1 12.0 1.0 CE1 B:HIS89 3.1 13.2 1.0 C1A B:HEM201 3.1 13.5 1.0 CD2 B:HIS89 3.1 14.4 1.0 CHD B:HEM201 3.4 14.9 1.0 CHA B:HEM201 3.4 13.4 1.0 CHC B:HEM201 3.4 12.1 1.0 CHB B:HEM201 3.4 11.9 1.0 O2 B:OXY202 3.9 15.8 1.0 ND1 B:HIS89 4.2 14.1 1.0 CG B:HIS89 4.2 13.3 1.0 C3C B:HEM201 4.3 13.7 1.0 C2D B:HEM201 4.3 16.1 1.0 C2C B:HEM201 4.3 13.1 1.0 C3D B:HEM201 4.3 16.1 1.0 C3A B:HEM201 4.3 13.7 1.0 C2B B:HEM201 4.3 11.3 1.0 C2A B:HEM201 4.3 13.8 1.0 C3B B:HEM201 4.3 11.0 1.0 CG2 B:VAL59 4.4 12.9 1.0 CE1 B:HIS55 4.6 15.8 1.0 CE B:MET86 4.9 17.9 1.0

Iron binding site 2 out of 3 in the Dehaloperoxidase A I9L Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Dehaloperoxidase A I9L Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:14.1 occ:0.43 FE A:HEM201 0.0 14.1 0.4 FE A:HEM201 0.1 9.9 0.6 NA A:HEM201 2.0 11.4 0.6 NA A:HEM201 2.0 13.0 0.4 NB A:HEM201 2.0 9.4 0.6 ND A:HEM201 2.0 14.3 0.4 NC A:HEM201 2.0 10.6 0.6 ND A:HEM201 2.0 11.1 0.6 NB A:HEM201 2.0 12.7 0.4 NC A:HEM201 2.1 13.9 0.4 NE2 A:HIS89 2.2 11.4 1.0 O1 A:OXY204 2.5 20.3 1.0 C1A A:HEM201 3.0 12.0 0.6 C4A A:HEM201 3.0 11.9 0.4 C1A A:HEM201 3.0 12.4 0.4 C4A A:HEM201 3.0 11.0 0.6 C4D A:HEM201 3.1 13.9 0.4 C4C A:HEM201 3.1 11.5 0.6 C4D A:HEM201 3.1 11.5 0.6 C1B A:HEM201 3.1 10.1 0.6 C1C A:HEM201 3.1 10.1 0.6 C4B A:HEM201 3.1 8.8 0.6 C4C A:HEM201 3.1 14.1 0.4 C1D A:HEM201 3.1 14.9 0.4 C1D A:HEM201 3.1 12.6 0.6 C1B A:HEM201 3.1 12.0 0.4 C1C A:HEM201 3.1 12.9 0.4 C4B A:HEM201 3.1 12.0 0.4 CE1 A:HIS89 3.2 12.4 1.0 CD2 A:HIS89 3.2 12.2 1.0 CHA A:HEM201 3.4 12.6 0.6 CHA A:HEM201 3.4 13.8 0.4 CHD A:HEM201 3.4 12.1 0.6 CHB A:HEM201 3.4 11.8 0.4 CHB A:HEM201 3.4 10.4 0.6 CHC A:HEM201 3.4 9.1 0.6 CHD A:HEM201 3.4 14.4 0.4 CHC A:HEM201 3.4 12.3 0.4 O2 A:OXY204 3.9 17.0 1.0 C3A A:HEM201 4.2 12.1 0.4 C2A A:HEM201 4.2 14.4 0.6 C2A A:HEM201 4.2 12.0 0.4 C3A A:HEM201 4.2 13.0 0.6 C3D A:HEM201 4.3 14.9 0.4 C3D A:HEM201 4.3 13.5 0.6 C3C A:HEM201 4.3 11.7 0.6 C2D A:HEM201 4.3 15.2 0.4 C3C A:HEM201 4.3 13.9 0.4 C2C A:HEM201 4.3 11.0 0.6 C3B A:HEM201 4.3 9.2 0.6 C2B A:HEM201 4.3 10.2 0.6 C2D A:HEM201 4.3 13.9 0.6 C2C A:HEM201 4.3 13.5 0.4 C3B A:HEM201 4.3 11.5 0.4 C2B A:HEM201 4.3 11.6 0.4 ND1 A:HIS89 4.3 12.8 1.0 CG2 A:VAL59 4.3 12.3 1.0 CG A:HIS89 4.4 12.1 1.0 CE1 A:HIS55 4.8 14.9 1.0 CE A:MET86 4.9 18.0 1.0

Iron binding site 3 out of 3 in the Dehaloperoxidase A I9L Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Dehaloperoxidase A I9L Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:9.9 occ:0.57 FE A:HEM201 0.0 9.9 0.6 FE A:HEM201 0.1 14.1 0.4 NC A:HEM201 2.0 10.6 0.6 ND A:HEM201 2.0 14.3 0.4 ND A:HEM201 2.0 11.1 0.6 NC A:HEM201 2.0 13.9 0.4 NA A:HEM201 2.0 11.4 0.6 NA A:HEM201 2.0 13.0 0.4 NB A:HEM201 2.0 9.4 0.6 NB A:HEM201 2.1 12.7 0.4 NE2 A:HIS89 2.1 11.4 1.0 O1 A:OXY204 2.6 20.3 1.0 C4C A:HEM201 3.0 11.5 0.6 C4C A:HEM201 3.0 14.1 0.4 C1A A:HEM201 3.0 12.0 0.6 C1D A:HEM201 3.0 14.9 0.4 C1D A:HEM201 3.0 12.6 0.6 C1C A:HEM201 3.0 10.1 0.6 C4D A:HEM201 3.0 13.9 0.4 C4D A:HEM201 3.1 11.5 0.6 C1C A:HEM201 3.1 12.9 0.4 C1A A:HEM201 3.1 12.4 0.4 C4A A:HEM201 3.1 11.9 0.4 C4B A:HEM201 3.1 8.8 0.6 C4A A:HEM201 3.1 11.0 0.6 CE1 A:HIS89 3.1 12.4 1.0 C4B A:HEM201 3.1 12.0 0.4 CD2 A:HIS89 3.1 12.2 1.0 C1B A:HEM201 3.1 10.1 0.6 C1B A:HEM201 3.1 12.0 0.4 CHD A:HEM201 3.4 12.1 0.6 CHD A:HEM201 3.4 14.4 0.4 CHA A:HEM201 3.4 12.6 0.6 CHC A:HEM201 3.4 9.1 0.6 CHA A:HEM201 3.4 13.8 0.4 CHC A:HEM201 3.4 12.3 0.4 CHB A:HEM201 3.5 11.8 0.4 CHB A:HEM201 3.5 10.4 0.6 O2 A:OXY204 4.0 17.0 1.0 ND1 A:HIS89 4.2 12.8 1.0 CG A:HIS89 4.2 12.1 1.0 C3C A:HEM201 4.2 11.7 0.6 C3C A:HEM201 4.3 13.9 0.4 C3D A:HEM201 4.3 14.9 0.4 C2D A:HEM201 4.3 15.2 0.4 C2C A:HEM201 4.3 11.0 0.6 C3D A:HEM201 4.3 13.5 0.6 C2A A:HEM201 4.3 14.4 0.6 C2C A:HEM201 4.3 13.5 0.4 C2D A:HEM201 4.3 13.9 0.6 C3A A:HEM201 4.3 12.1 0.4 C2A A:HEM201 4.3 12.0 0.4 C3A A:HEM201 4.3 13.0 0.6 C3B A:HEM201 4.3 9.2 0.6 C3B A:HEM201 4.3 11.5 0.4 C2B A:HEM201 4.3 10.2 0.6 C2B A:HEM201 4.3 11.6 0.4 CG2 A:VAL59 4.5 12.3 1.0 CE A:MET86 4.8 18.0 1.0 CE1 A:HIS55 4.9 14.9 1.0

L.M.Carey, R.Gavenko, D.A.Svistunenko, R.A.Ghiladi. How Nature Tunes Isoenzyme Activity in the Multifunctional Catalytic Globin Dehaloperoxidase From Amphitrite Ornata. Biochim Biophys Acta V.1866 230 2018PROTEINS Proteom.
ISSN: ISSN 1570-9639
PubMed: 29128676
DOI: 10.1016/J.BBAPAP.2017.11.004