Iron in PDB 8k1x: Biochemical and Structural Characterization of A Multifunctional Cytochrome P450 Spcn in Staurosporine Biosynthesis

The structure of Biochemical and Structural Characterization of A Multifunctional Cytochrome P450 Spcn in Staurosporine Biosynthesis, PDB code: 8k1x was solved by F.Xiao, S.Dong, Y.Feng, W.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.17 / 2.27
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	206.96, 121.79, 64.21, 90, 91.45, 90
R / Rfree (%)	21.1 / 23.4

The binding sites of Iron atom in the Biochemical and Structural Characterization of A Multifunctional Cytochrome P450 Spcn in Staurosporine Biosynthesis (pdb code 8k1x). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Biochemical and Structural Characterization of A Multifunctional Cytochrome P450 Spcn in Staurosporine Biosynthesis, PDB code: 8k1x:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Biochemical and Structural Characterization of A Multifunctional Cytochrome P450 Spcn in Staurosporine Biosynthesis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Biochemical and Structural Characterization of A Multifunctional Cytochrome P450 Spcn in Staurosporine Biosynthesis within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:36.7 occ:1.00 FE A:HEM501 0.0 36.7 1.0 ND A:HEM501 1.8 54.1 1.0 NA A:HEM501 1.9 43.1 1.0 NC A:HEM501 2.0 47.7 1.0 NB A:HEM501 2.1 52.5 1.0 SG A:CYS357 2.7 50.0 1.0 C4D A:HEM501 2.8 55.2 1.0 C1D A:HEM501 2.9 49.1 1.0 C1A A:HEM501 2.9 47.3 1.0 C4C A:HEM501 3.0 47.9 1.0 C4A A:HEM501 3.0 42.1 1.0 C4B A:HEM501 3.0 47.2 1.0 C1C A:HEM501 3.0 47.0 1.0 C1B A:HEM501 3.0 49.9 1.0 CHA A:HEM501 3.2 52.1 1.0 CHD A:HEM501 3.4 47.3 1.0 CHC A:HEM501 3.4 41.5 1.0 CHB A:HEM501 3.4 43.0 1.0 CB A:CYS357 3.4 49.5 1.0 C3D A:HEM501 4.0 57.0 1.0 O A:HOH632 4.0 48.4 1.0 C2D A:HEM501 4.1 54.4 1.0 C2A A:HEM501 4.1 45.6 1.0 C3A A:HEM501 4.1 45.4 1.0 C3C A:HEM501 4.1 44.1 1.0 CA A:CYS357 4.1 48.1 1.0 C2C A:HEM501 4.1 44.8 1.0 C2B A:HEM501 4.2 47.2 1.0 C3B A:HEM501 4.2 47.5 1.0 C21 A:VI4502 4.7 50.0 1.0 N A:GLY359 4.8 49.8 1.0 C22 A:VI4502 4.8 48.1 1.0 N A:ILE358 4.8 48.2 1.0 C A:CYS357 4.9 48.2 1.0

Iron binding site 2 out of 3 in the Biochemical and Structural Characterization of A Multifunctional Cytochrome P450 Spcn in Staurosporine Biosynthesis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Biochemical and Structural Characterization of A Multifunctional Cytochrome P450 Spcn in Staurosporine Biosynthesis within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:46.3 occ:1.00 FE B:HEM501 0.0 46.3 1.0 ND B:HEM501 1.8 54.2 1.0 NA B:HEM501 1.9 43.5 1.0 NC B:HEM501 2.0 49.0 1.0 NB B:HEM501 2.0 51.0 1.0 C4D B:HEM501 2.8 53.5 1.0 C1A B:HEM501 2.8 47.8 1.0 C1D B:HEM501 2.8 53.8 1.0 SG B:CYS357 2.8 59.4 1.0 C4C B:HEM501 2.9 50.7 1.0 C4A B:HEM501 2.9 42.3 1.0 C1B B:HEM501 3.0 51.0 1.0 C4B B:HEM501 3.0 50.4 1.0 C1C B:HEM501 3.0 53.1 1.0 CHA B:HEM501 3.2 50.0 1.0 CHD B:HEM501 3.3 54.5 1.0 CB B:CYS357 3.3 53.5 1.0 CHB B:HEM501 3.3 47.6 1.0 CHC B:HEM501 3.4 49.4 1.0 O B:HOH619 3.9 56.9 1.0 C2A B:HEM501 4.0 52.4 1.0 C3A B:HEM501 4.0 49.8 1.0 C3D B:HEM501 4.0 56.8 1.0 C2D B:HEM501 4.0 55.3 1.0 C3C B:HEM501 4.1 52.1 1.0 CA B:CYS357 4.1 54.0 1.0 C2C B:HEM501 4.1 52.5 1.0 C2B B:HEM501 4.1 49.7 1.0 C3B B:HEM501 4.2 48.7 1.0 C21 B:VI4502 4.5 59.8 1.0 C22 B:VI4502 4.7 61.1 1.0 C B:CYS357 4.9 60.3 1.0 N B:GLY359 5.0 58.1 1.0

Iron binding site 3 out of 3 in the Biochemical and Structural Characterization of A Multifunctional Cytochrome P450 Spcn in Staurosporine Biosynthesis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Biochemical and Structural Characterization of A Multifunctional Cytochrome P450 Spcn in Staurosporine Biosynthesis within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:43.5 occ:1.00 FE C:HEM501 0.0 43.5 1.0 ND C:HEM501 1.8 53.9 1.0 NA C:HEM501 1.9 45.7 1.0 NC C:HEM501 2.0 50.3 1.0 NB C:HEM501 2.0 48.3 1.0 C4D C:HEM501 2.8 53.0 1.0 C1D C:HEM501 2.8 55.4 1.0 SG C:CYS357 2.8 58.5 1.0 C1A C:HEM501 2.9 49.2 1.0 C4B C:HEM501 2.9 48.4 1.0 C4A C:HEM501 3.0 40.6 1.0 C4C C:HEM501 3.0 49.2 1.0 C1C C:HEM501 3.0 49.5 1.0 C1B C:HEM501 3.0 49.5 1.0 CHA C:HEM501 3.2 47.9 1.0 CHD C:HEM501 3.3 52.6 1.0 CHC C:HEM501 3.3 44.7 1.0 CB C:CYS357 3.4 56.2 1.0 CHB C:HEM501 3.4 44.4 1.0 O C:HOH626 3.6 57.8 1.0 C2D C:HEM501 4.0 57.9 1.0 C3D C:HEM501 4.0 57.8 1.0 C2A C:HEM501 4.0 51.3 1.0 C3A C:HEM501 4.1 48.4 1.0 CA C:CYS357 4.1 55.5 1.0 C2C C:HEM501 4.1 50.5 1.0 C3C C:HEM501 4.1 48.7 1.0 C3B C:HEM501 4.1 50.5 1.0 C2B C:HEM501 4.1 47.2 1.0 C21 C:VI4502 4.8 48.7 1.0 N C:GLY359 4.8 62.6 1.0 C22 C:VI4502 4.8 52.5 1.0 C C:CYS357 4.8 56.9 1.0 N C:ILE358 4.8 55.8 1.0

F.Xiao, S.Dong, Y.Feng, W.Li. Molecular Basis For the P450-Catalyzed SP3 C-N Glycosidic Bond Formation in Staurosporine Biosynthesis. Acs Catalysis V. 14 14274 2024.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.4C03875