Iron in PDB 5y5f: Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray

All present enzymatic activity of Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray:
1.7.1.14;

The structure of Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray, PDB code: 5y5f was solved by T.Tosha, T.Nomura, T.Nishida, G.Ueno, H.Murakami, K.Yamashita, K.Hirata, M.Yamamoto, H.Ago, H.Sugimoto, Y.Shiro, M.Kubo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.97 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.916, 75.667, 101.811, 90.00, 90.00, 90.00
R / Rfree (%)	16.1 / 18.6

The binding sites of Iron atom in the Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray (pdb code 5y5f). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray, PDB code: 5y5f:

Iron binding site 1 out of 1 in the Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:11.0 occ:1.00 FE A:HEM501 0.0 11.0 1.0 N A:NO502 1.7 14.2 1.0 NA A:HEM501 2.0 10.5 1.0 ND A:HEM501 2.0 10.4 1.0 NC A:HEM501 2.0 10.6 1.0 NB A:HEM501 2.1 9.1 1.0 SG A:CYS352 2.4 10.3 1.0 O A:NO502 2.8 17.2 1.0 C1A A:HEM501 3.0 9.8 1.0 C4A A:HEM501 3.0 10.0 1.0 C4C A:HEM501 3.0 10.0 1.0 C1D A:HEM501 3.0 9.9 1.0 C4D A:HEM501 3.0 10.3 1.0 C1C A:HEM501 3.1 12.6 1.0 C1B A:HEM501 3.1 11.0 1.0 C4B A:HEM501 3.1 10.7 1.0 HB2 A:CYS352 3.3 12.7 1.0 CHD A:HEM501 3.4 11.6 1.0 CHB A:HEM501 3.4 9.2 1.0 CHA A:HEM501 3.4 9.3 1.0 CHC A:HEM501 3.4 11.9 1.0 CB A:CYS352 3.5 10.6 1.0 HA A:CYS352 4.0 11.8 1.0 HB3 A:CYS352 4.2 12.7 1.0 C2A A:HEM501 4.2 11.1 1.0 C3A A:HEM501 4.2 9.1 1.0 C3C A:HEM501 4.2 11.2 1.0 C2D A:HEM501 4.3 10.6 1.0 C3D A:HEM501 4.3 10.2 1.0 C2C A:HEM501 4.3 11.2 1.0 C3B A:HEM501 4.3 9.6 1.0 C2B A:HEM501 4.3 11.1 1.0 CA A:CYS352 4.3 9.8 1.0 HHD A:HEM501 4.4 13.9 1.0 HHB A:HEM501 4.4 11.1 1.0 HHA A:HEM501 4.4 11.2 1.0 HHC A:HEM501 4.4 14.3 1.0 CA A:GLY240 4.6 11.3 1.0 O A:HOH885 4.7 23.1 1.0 O A:ALA239 4.9 11.7 1.0

T.Tosha, T.Nomura, T.Nishida, N.Saeki, K.Okubayashi, R.Yamagiwa, M.Sugahara, T.Nakane, K.Yamashita, K.Hirata, G.Ueno, T.Kimura, T.Hisano, K.Muramoto, H.Sawai, H.Takeda, E.Mizohata, A.Yamashita, Y.Kanematsu, Y.Takano, E.Nango, R.Tanaka, O.Nureki, O.Shoji, Y.Ikemoto, H.Murakami, S.Owada, K.Tono, M.Yabashi, M.Yamamoto, H.Ago, S.Iwata, H.Sugimoto, Y.Shiro, M.Kubo. Capturing An Initial Intermediate During the P450NOR Enzymatic Reaction Using Time-Resolved Xfel Crystallography and Caged-Substrate. Nat Commun V. 8 1585 2017.
ISSN: ESSN 2041-1723
PubMed: 29147002
DOI: 10.1038/S41467-017-01702-1