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Iron in PDB 4l0e: Structure of P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis (Heme-Coordinated Expression Tag)

Protein crystallography data

The structure of Structure of P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis (Heme-Coordinated Expression Tag), PDB code: 4l0e was solved by M.J.Cryle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.94 / 2.70
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.620, 91.620, 123.330, 90.00, 90.00, 120.00
R / Rfree (%) 24.8 / 29.3

Iron Binding Sites:

The binding sites of Iron atom in the Structure of P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis (Heme-Coordinated Expression Tag) (pdb code 4l0e). 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 P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis (Heme-Coordinated Expression Tag), PDB code: 4l0e:

Iron binding site 1 out of 1 in 4l0e

Go back to Iron Binding Sites List in 4l0e
Iron binding site 1 out of 1 in the Structure of P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis (Heme-Coordinated Expression Tag)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of P450SKY (CYP163B3), A Cytochrome P450 From Skyllamycin Biosynthesis (Heme-Coordinated Expression Tag) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:30.9
occ:1.00
FE A:HEM501 0.0 30.9 1.0
NA A:HEM501 2.0 30.4 1.0
NB A:HEM501 2.0 29.8 1.0
NC A:HEM501 2.0 30.1 1.0
ND A:HEM501 2.1 30.4 1.0
SG A:CYS357 2.4 35.1 1.0
C4A A:HEM501 3.0 30.5 1.0
C1B A:HEM501 3.0 30.3 1.0
C4C A:HEM501 3.1 30.3 1.0
C4B A:HEM501 3.1 30.0 1.0
C1A A:HEM501 3.1 30.7 1.0
C1C A:HEM501 3.1 30.1 1.0
C4D A:HEM501 3.1 30.9 1.0
C1D A:HEM501 3.1 30.1 1.0
CHB A:HEM501 3.4 30.5 1.0
CHC A:HEM501 3.4 30.2 1.0
CHD A:HEM501 3.4 29.7 1.0
CHA A:HEM501 3.4 30.9 1.0
CB A:CYS357 3.5 36.3 1.0
CA A:CYS357 4.2 37.8 1.0
C3A A:HEM501 4.3 30.1 1.0
C3C A:HEM501 4.3 29.9 1.0
C2C A:HEM501 4.3 29.9 1.0
C2B A:HEM501 4.3 30.3 1.0
C2A A:HEM501 4.3 30.4 1.0
C3B A:HEM501 4.3 30.0 1.0
C3D A:HEM501 4.3 31.1 1.0
C2D A:HEM501 4.4 30.3 1.0
O A:GLY247 4.8 38.0 1.0
N A:LEU358 4.9 38.4 1.0
N A:GLY359 4.9 36.5 1.0
C A:CYS357 4.9 38.4 1.0

Reference:

S.Uhlmann, R.D.Sussmuth, M.J.Cryle. Cytochrome P450SKY Interacts Directly with the Nonribosomal Peptide Synthetase to Generate Three Amino Acid Precursors in Skyllamycin Biosynthesis. Acs Chem.Biol. V. 8 2586 2013.
ISSN: ISSN 1554-8929
PubMed: 24079328
DOI: 10.1021/CB400555E
Page generated: Sun Dec 13 15:40:23 2020

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