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Iron in PDB 1s1f: Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 From Antibiotic Biosynthetic Pathways

Protein crystallography data

The structure of Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 From Antibiotic Biosynthetic Pathways, PDB code: 1s1f was solved by B.Zhao, D.C.Lamb, L.Lei, M.Sundaramoorthy, L.M.Podust, M.R.Waterman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.26 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.250, 65.553, 104.245, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 21.6

Other elements in 1s1f:

The structure of Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 From Antibiotic Biosynthetic Pathways also contains other interesting chemical elements:

Mercury (Hg) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 From Antibiotic Biosynthetic Pathways (pdb code 1s1f). 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 Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 From Antibiotic Biosynthetic Pathways, PDB code: 1s1f:

Iron binding site 1 out of 1 in 1s1f

Go back to Iron Binding Sites List in 1s1f
Iron binding site 1 out of 1 in the Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 From Antibiotic Biosynthetic Pathways


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 From Antibiotic Biosynthetic Pathways within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe430

b:11.8
occ:1.00
FE A:HEM430 0.0 11.8 1.0
ND A:HEM430 2.0 12.1 1.0
NC A:HEM430 2.0 11.6 1.0
NB A:HEM430 2.0 10.8 1.0
NA A:HEM430 2.0 11.9 1.0
N3 A:PIM431 2.2 15.0 1.0
SG A:CYS353 2.3 11.5 1.0
C4D A:HEM430 3.0 11.1 1.0
C1C A:HEM430 3.0 10.5 1.0
C1D A:HEM430 3.1 12.5 1.0
C2 A:PIM431 3.1 15.4 1.0
C1A A:HEM430 3.1 12.2 1.0
C1B A:HEM430 3.1 11.2 1.0
C4C A:HEM430 3.1 13.1 1.0
C4A A:HEM430 3.1 11.8 1.0
C4B A:HEM430 3.1 11.2 1.0
C4 A:PIM431 3.3 15.7 1.0
CB A:CYS353 3.4 11.8 1.0
CHA A:HEM430 3.4 11.3 1.0
CHD A:HEM430 3.4 12.8 1.0
CHB A:HEM430 3.4 12.4 1.0
CHC A:HEM430 3.4 11.2 1.0
C3D A:HEM430 4.3 11.3 1.0
C2D A:HEM430 4.3 12.8 1.0
N1 A:PIM431 4.3 16.1 1.0
C3A A:HEM430 4.3 11.6 1.0
C2A A:HEM430 4.3 11.5 1.0
CA A:CYS353 4.3 12.1 1.0
C3C A:HEM430 4.3 12.8 1.0
C2C A:HEM430 4.3 12.6 1.0
C2B A:HEM430 4.3 11.9 1.0
C3B A:HEM430 4.3 12.4 1.0
C5 A:PIM431 4.4 17.3 1.0

Reference:

B.Zhao, F.P.Guengerich, A.Bellamine, D.C.Lamb, M.Izumikawa, L.Lei, L.M.Podust, M.Sundaramoorthy, J.A.Kalaitzis, L.M.Reddy, S.L.Kelly, B.S.Moore, D.Stec, M.Voehler, J.R.Falck, T.Shimada, M.R.Waterman. Binding of Two Flaviolin Substrate Molecules, Oxidative Coupling, and Crystal Structure of Streptomyces Coelicolor A3(2) Cytochrome P450 158A2 J.Biol.Chem. V. 280 11599 2005.
ISSN: ISSN 0021-9258
PubMed: 15659395
DOI: 10.1074/JBC.M410933200
Page generated: Sun Dec 13 14:31:07 2020

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