Iron in PDB 1ued: Crystal Structure of Oxyc A Cytochrome P450 Implicated in An Oxidative C-C Coupling Reaction During Vancomycin Biosynthesis.

The structure of Crystal Structure of Oxyc A Cytochrome P450 Implicated in An Oxidative C-C Coupling Reaction During Vancomycin Biosynthesis., PDB code: 1ued was solved by O.Pylypenko, F.Vitali, K.Zerbe, J.A.Robinson, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.063, 99.270, 105.081, 90.00, 96.11, 90.00
R / Rfree (%)	19.6 / 23.5

The binding sites of Iron atom in the Crystal Structure of Oxyc A Cytochrome P450 Implicated in An Oxidative C-C Coupling Reaction During Vancomycin Biosynthesis. (pdb code 1ued). 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 Oxyc A Cytochrome P450 Implicated in An Oxidative C-C Coupling Reaction During Vancomycin Biosynthesis., PDB code: 1ued:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Oxyc A Cytochrome P450 Implicated in An Oxidative C-C Coupling Reaction During Vancomycin Biosynthesis.


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 Oxyc A Cytochrome P450 Implicated in An Oxidative C-C Coupling Reaction During Vancomycin Biosynthesis. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1430 b:14.4 occ:1.00 FE A:HEM1430 0.0 14.4 1.0 NB A:HEM1430 2.0 10.9 1.0 NC A:HEM1430 2.0 14.3 1.0 ND A:HEM1430 2.0 14.3 1.0 NA A:HEM1430 2.0 13.1 1.0 SG A:CYS356 2.4 15.1 1.0 O A:HOH4518 2.5 23.8 1.0 C4A A:HEM1430 3.0 10.8 1.0 C1B A:HEM1430 3.0 11.5 1.0 C4C A:HEM1430 3.0 14.3 1.0 C4B A:HEM1430 3.1 10.4 1.0 C1C A:HEM1430 3.1 13.6 1.0 C1D A:HEM1430 3.1 11.9 1.0 C1A A:HEM1430 3.1 12.2 1.0 C4D A:HEM1430 3.1 13.0 1.0 CHB A:HEM1430 3.3 9.7 1.0 CB A:CYS356 3.4 10.1 1.0 CHD A:HEM1430 3.4 14.1 1.0 CHA A:HEM1430 3.5 14.0 1.0 CHC A:HEM1430 3.5 11.5 1.0 O A:GLY245 3.9 16.0 1.0 CA A:CYS356 4.0 12.8 1.0 C3B A:HEM1430 4.2 10.9 1.0 C2B A:HEM1430 4.3 9.5 1.0 C3A A:HEM1430 4.3 13.6 1.0 C2D A:HEM1430 4.3 11.7 1.0 C2C A:HEM1430 4.3 13.4 1.0 C3C A:HEM1430 4.3 15.3 1.0 C2A A:HEM1430 4.3 11.9 1.0 C3D A:HEM1430 4.3 12.7 1.0 C1 A:PG44502 4.7 41.8 1.0 C A:GLY245 4.7 17.9 1.0 C A:CYS356 4.8 13.4 1.0 N A:GLY358 4.8 13.7 1.0 N A:VAL357 4.9 13.7 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Oxyc A Cytochrome P450 Implicated in An Oxidative C-C Coupling Reaction During Vancomycin Biosynthesis.


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 Oxyc A Cytochrome P450 Implicated in An Oxidative C-C Coupling Reaction During Vancomycin Biosynthesis. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2430 b:17.7 occ:1.00 FE B:HEM2430 0.0 17.7 1.0 NB B:HEM2430 2.0 15.8 1.0 ND B:HEM2430 2.0 14.1 1.0 NA B:HEM2430 2.1 14.9 1.0 NC B:HEM2430 2.1 14.8 1.0 SG B:CYS356 2.4 18.0 1.0 O B:HOH5680 2.5 29.2 1.0 C4B B:HEM2430 3.0 16.5 1.0 C4D B:HEM2430 3.1 12.6 1.0 C1B B:HEM2430 3.1 16.5 1.0 C1D B:HEM2430 3.1 15.8 1.0 C4A B:HEM2430 3.1 16.4 1.0 C1C B:HEM2430 3.1 16.5 1.0 C1A B:HEM2430 3.1 15.4 1.0 C4C B:HEM2430 3.1 16.8 1.0 CB B:CYS356 3.4 15.3 1.0 CHB B:HEM2430 3.4 15.1 1.0 CHC B:HEM2430 3.4 13.7 1.0 CHA B:HEM2430 3.5 15.0 1.0 CHD B:HEM2430 3.5 15.2 1.0 O B:GLY245 4.0 20.0 1.0 CA B:CYS356 4.1 15.1 1.0 C3B B:HEM2430 4.2 15.8 1.0 C3D B:HEM2430 4.3 13.8 1.0 C2B B:HEM2430 4.3 17.0 1.0 C2D B:HEM2430 4.3 15.4 1.0 C2A B:HEM2430 4.4 15.2 1.0 C3A B:HEM2430 4.4 14.8 1.0 C3C B:HEM2430 4.4 13.8 1.0 C2C B:HEM2430 4.4 13.2 1.0 C B:GLY245 4.7 19.4 1.0 C B:CYS356 4.8 16.8 1.0 N B:GLY358 4.9 18.3 1.0 O1 B:PG45502 4.9 56.3 1.0 N B:VAL357 4.9 18.3 1.0

O.Pylypenko, F.Vitali, K.Zerbe, J.A.Robinson, I.Schlichting. Crystal Structure of Oxyc, A Cytochrome P450 Implicated in An Oxidative C-C Coupling Reaction During Vancomycin Biosynthesis J.Biol.Chem. V. 278 46727 2003.
ISSN: ISSN 0021-9258
PubMed: 12888556
DOI: 10.1074/JBC.M306486200