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Iron in PDB 1jme: Crystal Structure of PHE393HIS Cytochrome P450 BM3

Enzymatic activity of Crystal Structure of PHE393HIS Cytochrome P450 BM3

All present enzymatic activity of Crystal Structure of PHE393HIS Cytochrome P450 BM3:
1.14.14.1;

Protein crystallography data

The structure of Crystal Structure of PHE393HIS Cytochrome P450 BM3, PDB code: 1jme was solved by T.W.B.Ost, A.W.Munro, C.G.Mowat, A.Pesseguiero, A.J.Fulco, A.K.Cho, M.A.Cheesman, M.D.Walkinshaw, S.K.Chapman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.842, 153.102, 61.479, 90.00, 94.67, 90.00
R / Rfree (%) 17.9 / 23.1

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of PHE393HIS Cytochrome P450 BM3 (pdb code 1jme). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of PHE393HIS Cytochrome P450 BM3, PDB code: 1jme:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1jme

Go back to Iron Binding Sites List in 1jme
Iron binding site 1 out of 2 in the Crystal Structure of PHE393HIS Cytochrome P450 BM3


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 PHE393HIS Cytochrome P450 BM3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe460

b:16.8
occ:1.00
FE A:HEM460 0.0 16.8 1.0
O A:HOH469 1.8 21.2 1.0
NB A:HEM460 1.9 20.5 1.0
NA A:HEM460 2.0 17.0 1.0
NC A:HEM460 2.0 17.2 1.0
ND A:HEM460 2.0 22.5 1.0
SG A:CYS400 2.1 17.0 1.0
C4B A:HEM460 3.0 14.7 1.0
C1B A:HEM460 3.0 20.0 1.0
C1C A:HEM460 3.0 21.6 1.0
C4A A:HEM460 3.0 19.2 1.0
C1A A:HEM460 3.1 19.6 1.0
C4D A:HEM460 3.1 20.2 1.0
C4C A:HEM460 3.1 15.2 1.0
C1D A:HEM460 3.1 21.0 1.0
CB A:CYS400 3.2 19.8 1.0
CHC A:HEM460 3.3 16.8 1.0
CHB A:HEM460 3.4 18.7 1.0
CHA A:HEM460 3.4 19.3 1.0
CHD A:HEM460 3.4 16.2 1.0
O A:HOH796 3.8 30.2 1.0
CA A:CYS400 4.0 19.1 1.0
C3B A:HEM460 4.2 16.8 1.0
C2B A:HEM460 4.2 15.4 1.0
C3A A:HEM460 4.3 21.1 1.0
C2C A:HEM460 4.3 18.4 1.0
C2A A:HEM460 4.3 17.7 1.0
C3C A:HEM460 4.3 15.7 1.0
O A:ALA264 4.3 24.6 1.0
C2D A:HEM460 4.3 21.4 1.0
C3D A:HEM460 4.3 17.8 1.0
CB A:ALA264 4.7 17.8 1.0
C A:CYS400 4.8 17.0 1.0
CD2 A:HIS393 4.8 17.9 1.0
N A:GLY402 4.8 16.0 1.0
C A:ALA264 4.9 16.8 1.0
N A:ILE401 5.0 15.2 1.0

Iron binding site 2 out of 2 in 1jme

Go back to Iron Binding Sites List in 1jme
Iron binding site 2 out of 2 in the Crystal Structure of PHE393HIS Cytochrome P450 BM3


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of PHE393HIS Cytochrome P450 BM3 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe460

b:17.7
occ:1.00
FE B:HEM460 0.0 17.7 1.0
O B:HOH714 1.8 27.6 1.0
NC B:HEM460 2.0 18.6 1.0
NB B:HEM460 2.0 18.9 1.0
ND B:HEM460 2.0 21.5 1.0
NA B:HEM460 2.1 21.9 1.0
SG B:CYS400 2.1 18.0 1.0
C1C B:HEM460 3.0 20.0 1.0
C4C B:HEM460 3.0 20.7 1.0
C4B B:HEM460 3.0 20.1 1.0
C1D B:HEM460 3.1 23.4 1.0
C1B B:HEM460 3.1 20.8 1.0
C4A B:HEM460 3.1 18.4 1.0
C1A B:HEM460 3.1 22.9 1.0
C4D B:HEM460 3.1 22.1 1.0
CB B:CYS400 3.2 20.2 1.0
CHC B:HEM460 3.3 20.9 1.0
CHD B:HEM460 3.4 18.3 1.0
CHB B:HEM460 3.4 15.3 1.0
CHA B:HEM460 3.5 19.4 1.0
CA B:CYS400 3.9 21.7 1.0
C2C B:HEM460 4.2 19.1 1.0
C3C B:HEM460 4.2 21.3 1.0
C3B B:HEM460 4.3 21.5 1.0
C2B B:HEM460 4.3 19.8 1.0
O B:ALA264 4.3 17.5 1.0
C2D B:HEM460 4.3 26.9 1.0
C3A B:HEM460 4.3 24.4 1.0
C2A B:HEM460 4.3 23.2 1.0
C3D B:HEM460 4.3 21.3 1.0
O B:HOH606 4.4 29.9 1.0
C B:CYS400 4.7 16.2 1.0
N B:GLY402 4.7 19.2 1.0
CB B:ALA264 4.8 21.4 1.0
N B:ILE401 4.9 13.8 1.0
CD2 B:HIS393 4.9 19.2 1.0
C B:ALA264 4.9 21.3 1.0

Reference:

T.W.Ost, A.W.Munro, C.G.Mowat, P.R.Taylor, A.Pesseguiero, A.J.Fulco, A.K.Cho, M.A.Cheesman, M.D.Walkinshaw, S.K.Chapman. Structural and Spectroscopic Analysis of the F393H Mutant of Flavocytochrome P450 BM3. Biochemistry V. 40 13430 2001.
ISSN: ISSN 0006-2960
PubMed: 11695889
DOI: 10.1021/BI010717E
Page generated: Sat Aug 3 08:35:21 2024

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