Iron in PDB 1gjm: Covalent Attachment of An Electroactive Sulphydryl Reagent in the Active Site of Cytochrome P450CAM

All present enzymatic activity of Covalent Attachment of An Electroactive Sulphydryl Reagent in the Active Site of Cytochrome P450CAM:
1.14.15.1;

The structure of Covalent Attachment of An Electroactive Sulphydryl Reagent in the Active Site of Cytochrome P450CAM, PDB code: 1gjm was solved by V.Fulop, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.0 / 2.2
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.100, 61.100, 215.400, 90.00, 90.00, 120.00
R / Rfree (%)	18.3 / 22.1

The binding sites of Iron atom in the Covalent Attachment of An Electroactive Sulphydryl Reagent in the Active Site of Cytochrome P450CAM (pdb code 1gjm). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Covalent Attachment of An Electroactive Sulphydryl Reagent in the Active Site of Cytochrome P450CAM, PDB code: 1gjm:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Covalent Attachment of An Electroactive Sulphydryl Reagent in the Active Site of Cytochrome P450CAM


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Covalent Attachment of An Electroactive Sulphydryl Reagent in the Active Site of Cytochrome P450CAM within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe417 b:10.4 occ:1.00 FE A:HEM417 0.0 10.4 1.0 NA A:HEM417 2.0 7.3 1.0 NB A:HEM417 2.0 6.6 1.0 ND A:HEM417 2.0 5.8 1.0 NC A:HEM417 2.0 6.3 1.0 SG A:CYS357 2.2 11.0 1.0 O A:HOH2314 2.5 23.9 1.0 C1B A:HEM417 3.0 9.1 1.0 C1D A:HEM417 3.0 5.3 1.0 C4A A:HEM417 3.0 7.9 1.0 C4C A:HEM417 3.0 7.9 1.0 C1C A:HEM417 3.0 8.6 1.0 C4D A:HEM417 3.0 5.5 1.0 C1A A:HEM417 3.1 4.5 1.0 C4B A:HEM417 3.1 7.2 1.0 CB A:CYS357 3.4 8.3 1.0 CHB A:HEM417 3.4 6.8 1.0 CHD A:HEM417 3.4 8.8 1.0 CHC A:HEM417 3.4 8.2 1.0 CHA A:HEM417 3.4 7.0 1.0 CA A:CYS357 4.1 11.4 1.0 C2D A:HEM417 4.3 7.1 1.0 C3A A:HEM417 4.3 4.6 1.0 C2B A:HEM417 4.3 7.0 1.0 C2A A:HEM417 4.3 4.5 1.0 C3D A:HEM417 4.3 7.3 1.0 C2C A:HEM417 4.3 7.3 1.0 C3C A:HEM417 4.3 6.2 1.0 C3B A:HEM417 4.3 5.5 1.0 N A:GLY359 4.9 12.0 1.0 C A:CYS357 4.9 13.4 1.0 OG1 A:THR252 4.9 17.4 1.0 N A:LEU358 5.0 13.3 1.0

Iron binding site 2 out of 3 in the Covalent Attachment of An Electroactive Sulphydryl Reagent in the Active Site of Cytochrome P450CAM


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Covalent Attachment of An Electroactive Sulphydryl Reagent in the Active Site of Cytochrome P450CAM within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe418 b:21.6 occ:1.00 FE A:FEM418 0.0 21.6 1.0 C1 A:FEM418 2.1 22.1 1.0 C5 A:FEM418 2.1 23.1 1.0 C2 A:FEM418 2.1 21.4 1.0 C6 A:FEM418 2.1 23.2 1.0 C10 A:FEM418 2.1 24.3 1.0 C4 A:FEM418 2.1 23.3 1.0 C3 A:FEM418 2.1 21.7 1.0 C7 A:FEM418 2.1 22.0 1.0 C9 A:FEM418 2.1 22.0 1.0 C8 A:FEM418 2.1 22.5 1.0 C11 A:FEM418 3.2 17.3 1.0 CG1 A:VAL247 4.3 15.3 1.0 C12 A:FEM418 4.5 18.2 1.0 CD1 A:LEU244 4.7 11.8 1.0 CG2 A:ILE395 4.9 9.8 1.0

Iron binding site 3 out of 3 in the Covalent Attachment of An Electroactive Sulphydryl Reagent in the Active Site of Cytochrome P450CAM


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Covalent Attachment of An Electroactive Sulphydryl Reagent in the Active Site of Cytochrome P450CAM within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe419 b:52.8 occ:1.00 FE A:FEM419 0.0 52.8 1.0 C1 A:FEM419 2.1 44.9 1.0 C6 A:FEM419 2.1 47.1 1.0 C2 A:FEM419 2.1 45.5 1.0 C3 A:FEM419 2.1 46.6 1.0 C7 A:FEM419 2.1 45.7 1.0 C8 A:FEM419 2.1 44.9 1.0 C4 A:FEM419 2.1 46.4 1.0 C5 A:FEM419 2.1 45.2 1.0 C9 A:FEM419 2.1 43.8 1.0 C10 A:FEM419 2.1 44.6 1.0 C11 A:FEM419 3.0 44.1 1.0 C12 A:FEM419 4.4 44.9 1.0

K.Digleria, D.P.Nickerson, H.A.O.Hill, L.-L.Wong, V.Fulop. Covalent Attachment of An Electroactive Sulphydryl Reagent in the Active Site of Cytochrome P450CAM As Revealed By the Crystal Structure of the Modified Protein J.Am.Chem.Soc. V. 120 46 1998.
ISSN: ISSN 0002-7863