Iron in PDB 1dk0: Crystal Structure of the Hemophore Hasa From Serratia Marcescens Crystal Form P2(1), PH8

The structure of Crystal Structure of the Hemophore Hasa From Serratia Marcescens Crystal Form P2(1), PH8, PDB code: 1dk0 was solved by P.Arnoux, R.Haser, N.Izadi-Pruneyre, A.Lecroisey, M.Czjzek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.77
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.540, 66.210, 58.930, 90.00, 104.91, 90.00
R / Rfree (%)	16.9 / 21.3

The binding sites of Iron atom in the Crystal Structure of the Hemophore Hasa From Serratia Marcescens Crystal Form P2(1), PH8 (pdb code 1dk0). 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 the Hemophore Hasa From Serratia Marcescens Crystal Form P2(1), PH8, PDB code: 1dk0:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Hemophore Hasa From Serratia Marcescens Crystal Form P2(1), PH8


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 the Hemophore Hasa From Serratia Marcescens Crystal Form P2(1), PH8 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:15.4 occ:1.00 FE A:HEM200 0.0 15.4 1.0 NA A:HEM200 2.0 15.8 1.0 ND A:HEM200 2.0 15.2 1.0 NB A:HEM200 2.0 13.9 1.0 NC A:HEM200 2.0 13.3 1.0 OH A:TYR75 2.1 12.6 1.0 NE2 A:HIS32 2.1 14.0 1.0 CZ A:TYR75 3.0 13.4 1.0 C1A A:HEM200 3.0 14.4 1.0 C4C A:HEM200 3.0 15.3 1.0 C4A A:HEM200 3.0 14.7 1.0 C1B A:HEM200 3.0 16.1 1.0 C1C A:HEM200 3.0 14.0 1.0 C4D A:HEM200 3.0 17.9 1.0 C4B A:HEM200 3.0 14.9 1.0 C1D A:HEM200 3.1 16.5 1.0 CD2 A:HIS32 3.1 14.2 1.0 CE1 A:HIS32 3.1 15.4 1.0 CHA A:HEM200 3.4 15.7 1.0 CHD A:HEM200 3.4 14.7 1.0 CHB A:HEM200 3.4 14.9 1.0 CHC A:HEM200 3.4 14.7 1.0 CE1 A:TYR75 3.7 13.0 1.0 CE2 A:TYR75 3.8 10.8 1.0 ND1 A:HIS83 4.0 16.3 1.0 ND1 A:HIS32 4.2 14.0 1.0 CG A:HIS32 4.2 14.5 1.0 C2A A:HEM200 4.3 16.3 1.0 C2B A:HEM200 4.3 13.6 1.0 C3B A:HEM200 4.3 16.9 1.0 C3D A:HEM200 4.3 18.6 1.0 C3C A:HEM200 4.3 15.5 1.0 C3A A:HEM200 4.3 15.6 1.0 C2D A:HEM200 4.3 18.6 1.0 C2C A:HEM200 4.3 14.1 1.0 CG A:HIS83 4.7 15.5 1.0 CB A:HIS83 4.7 13.1 1.0 CE1 A:HIS83 4.8 18.5 1.0 CD1 A:TYR75 4.9 12.4 1.0 CD2 A:TYR75 5.0 13.4 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Hemophore Hasa From Serratia Marcescens Crystal Form P2(1), PH8


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 the Hemophore Hasa From Serratia Marcescens Crystal Form P2(1), PH8 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe200 b:15.3 occ:1.00 FE B:HEM200 0.0 15.3 1.0 NC B:HEM200 2.0 12.8 1.0 NB B:HEM200 2.0 13.6 1.0 ND B:HEM200 2.0 16.7 1.0 NA B:HEM200 2.0 14.4 1.0 OH B:TYR75 2.1 13.1 1.0 NE2 B:HIS32 2.1 15.4 1.0 CE1 B:HIS32 3.0 15.9 1.0 C4B B:HEM200 3.0 15.5 1.0 C1D B:HEM200 3.0 17.5 1.0 C4C B:HEM200 3.0 15.4 1.0 CZ B:TYR75 3.0 13.6 1.0 C1C B:HEM200 3.0 14.3 1.0 C4D B:HEM200 3.0 18.6 1.0 C1B B:HEM200 3.1 15.3 1.0 C1A B:HEM200 3.1 15.4 1.0 C4A B:HEM200 3.1 15.1 1.0 CD2 B:HIS32 3.2 14.3 1.0 CHC B:HEM200 3.4 15.6 1.0 CHD B:HEM200 3.4 16.4 1.0 CHA B:HEM200 3.4 17.5 1.0 CHB B:HEM200 3.5 14.8 1.0 CE2 B:TYR75 3.8 12.3 1.0 CE1 B:TYR75 3.8 13.1 1.0 ND1 B:HIS83 4.0 12.5 1.0 ND1 B:HIS32 4.2 14.9 1.0 C3B B:HEM200 4.2 17.1 1.0 C3C B:HEM200 4.2 15.2 1.0 C3D B:HEM200 4.3 19.9 1.0 C2D B:HEM200 4.3 19.4 1.0 C2C B:HEM200 4.3 14.0 1.0 C2B B:HEM200 4.3 14.2 1.0 CG B:HIS32 4.3 11.2 1.0 C2A B:HEM200 4.3 18.3 1.0 C3A B:HEM200 4.3 16.6 1.0 CE1 B:HIS83 4.7 16.8 1.0 CG B:HIS83 4.7 13.5 1.0 CB B:HIS83 4.8 11.8 1.0 CD2 B:TYR75 5.0 11.8 1.0 CD1 B:TYR75 5.0 11.8 1.0

P.Arnoux, R.Haser, N.Izadi-Pruneyre, A.Lecroisey, M.Czjzek. Functional Aspects of the Heme Bound Hemophore Hasa By Structural Analysis of Various Crystal Forms. Proteins V. 41 202 2000.
ISSN: ISSN 0887-3585
PubMed: 10966573
DOI: 10.1002/1097-0134(20001101)41:2<202::AID-PROT50>3.0.CO;2-8