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Iron in PDB 2dkk: Structure/Function Studies of Cytochrome P450 158A1 From Streptomyces Coelicolor A3(2)

Protein crystallography data

The structure of Structure/Function Studies of Cytochrome P450 158A1 From Streptomyces Coelicolor A3(2), PDB code: 2dkk was solved by B.Zhao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.99 / 1.97
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 103.968, 44.352, 102.107, 90.00, 114.44, 90.00
R / Rfree (%) 22.8 / 28.5

Iron Binding Sites:

The binding sites of Iron atom in the Structure/Function Studies of Cytochrome P450 158A1 From Streptomyces Coelicolor A3(2) (pdb code 2dkk). 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/Function Studies of Cytochrome P450 158A1 From Streptomyces Coelicolor A3(2), PDB code: 2dkk:

Iron binding site 1 out of 1 in 2dkk

Go back to Iron Binding Sites List in 2dkk
Iron binding site 1 out of 1 in the Structure/Function Studies of Cytochrome P450 158A1 From Streptomyces Coelicolor A3(2)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure/Function Studies of Cytochrome P450 158A1 From Streptomyces Coelicolor A3(2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe430

b:15.7
occ:1.00
FE A:HEM430 0.0 15.7 1.0
ND A:HEM430 2.0 13.8 1.0
NB A:HEM430 2.0 15.7 1.0
NC A:HEM430 2.0 12.0 1.0
NA A:HEM430 2.0 15.3 1.0
SG A:CYS356 2.4 17.7 1.0
N1 A:IMD431 2.4 32.1 1.0
C4D A:HEM430 3.0 15.6 1.0
C1B A:HEM430 3.0 14.9 1.0
C1A A:HEM430 3.0 17.0 1.0
C1D A:HEM430 3.0 13.9 1.0
C1C A:HEM430 3.0 13.7 1.0
C4B A:HEM430 3.1 13.8 1.0
C4A A:HEM430 3.1 15.7 1.0
C4C A:HEM430 3.1 11.5 1.0
C5 A:IMD431 3.2 32.8 1.0
CHA A:HEM430 3.4 16.8 1.0
CHB A:HEM430 3.4 15.0 1.0
CHD A:HEM430 3.4 12.7 1.0
CHC A:HEM430 3.4 11.0 1.0
CB A:CYS356 3.5 19.3 1.0
C2 A:IMD431 3.6 33.0 1.0
CA A:CYS356 4.2 19.1 1.0
C3D A:HEM430 4.3 15.0 1.0
C2B A:HEM430 4.3 14.4 1.0
C2D A:HEM430 4.3 14.2 1.0
C3B A:HEM430 4.3 14.2 1.0
C2A A:HEM430 4.3 15.9 1.0
C3A A:HEM430 4.3 16.8 1.0
C2C A:HEM430 4.3 11.0 1.0
C3C A:HEM430 4.3 12.8 1.0
C4 A:IMD431 4.4 33.5 1.0
O A:HOH705 4.5 25.3 1.0
N3 A:IMD431 4.6 33.9 1.0
C A:CYS356 4.9 18.5 1.0
N A:THR357 5.0 17.8 1.0

Reference:

B.Zhao, D.C.Lamb, L.Lei, S.L.Kelly, H.Yuan, D.L.Hachey, M.R.Waterman. Different Binding Modes of Two Flaviolin Substrate Molecules in Cytochrome P450 158A1 (CYP158A1) Compared to CYP158A2. Biochemistry V. 46 8725 2007.
ISSN: ISSN 0006-2960
PubMed: 17614370
DOI: 10.1021/BI7006959
Page generated: Sat Aug 3 20:47:31 2024

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