Iron in PDB 5h1z: CYP153D17 From Sphingomonas Sp. Pamc 26605

The structure of CYP153D17 From Sphingomonas Sp. Pamc 26605, PDB code: 5h1z was solved by C.W.Lee, J.H.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.01 / 3.10
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	110.837, 110.837, 113.180, 90.00, 90.00, 120.00
R / Rfree (%)	26.2 / 34

The binding sites of Iron atom in the CYP153D17 From Sphingomonas Sp. Pamc 26605 (pdb code 5h1z). 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 CYP153D17 From Sphingomonas Sp. Pamc 26605, PDB code: 5h1z:

Iron binding site 1 out of 1 in the CYP153D17 From Sphingomonas Sp. Pamc 26605


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of CYP153D17 From Sphingomonas Sp. Pamc 26605 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:68.1 occ:1.00 FE A:HEM501 0.0 68.1 1.0 ND A:HEM501 1.9 62.8 1.0 NA A:HEM501 2.0 67.2 1.0 NC A:HEM501 2.1 70.2 1.0 NB A:HEM501 2.1 65.6 1.0 SG A:CYS356 2.2 69.5 1.0 C1D A:HEM501 2.9 65.2 1.0 C4D A:HEM501 2.9 69.2 1.0 C1A A:HEM501 3.0 71.0 1.0 C4A A:HEM501 3.0 65.3 1.0 C1B A:HEM501 3.0 68.8 1.0 C4B A:HEM501 3.0 63.4 1.0 C4C A:HEM501 3.0 67.2 1.0 C1C A:HEM501 3.1 74.0 1.0 C1 A:D12502 3.1 87.5 1.0 CHA A:HEM501 3.4 71.8 1.0 CHD A:HEM501 3.4 64.7 1.0 CB A:CYS356 3.4 68.0 1.0 CHB A:HEM501 3.4 64.6 1.0 CHC A:HEM501 3.4 70.5 1.0 CA A:CYS356 4.1 62.8 1.0 C2D A:HEM501 4.1 76.4 1.0 C3D A:HEM501 4.1 74.8 1.0 C2A A:HEM501 4.2 76.2 1.0 C3A A:HEM501 4.2 73.5 1.0 C3C A:HEM501 4.3 68.3 1.0 C2B A:HEM501 4.3 67.0 1.0 C2C A:HEM501 4.3 69.5 1.0 C3B A:HEM501 4.3 64.8 1.0 CA A:GLY245 4.5 0.3 1.0 C2 A:D12502 4.5 85.7 1.0 C A:CYS356 4.8 60.4 1.0 O A:GLY245 5.0 0.8 1.0

C.W.Lee, S.C.Yu, J.H.Lee, S.H.Park, H.Park, T.J.Oh, J.H.Lee. Crystal Structure of A Putative Cytochrome P450 Alkane Hydroxylase (CYP153D17) From Sphingomonas Sp. Pamc 26605 and Its Conformational Substrate Binding Int J Mol Sci V. 17 2016.
ISSN: ESSN 1422-0067
PubMed: 27941697
DOI: 10.3390/IJMS17122067