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Iron in PDB 7yda: Crystal Structure of the P450 BM3 Heme Domain Mutant F87V/T268V/A184V in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine and Hydroxylamine

Enzymatic activity of Crystal Structure of the P450 BM3 Heme Domain Mutant F87V/T268V/A184V in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine and Hydroxylamine

All present enzymatic activity of Crystal Structure of the P450 BM3 Heme Domain Mutant F87V/T268V/A184V in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine and Hydroxylamine:
1.14.14.1; 1.6.2.4;

Protein crystallography data

The structure of Crystal Structure of the P450 BM3 Heme Domain Mutant F87V/T268V/A184V in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine and Hydroxylamine, PDB code: 7yda was solved by S.Dong, J.Chen, Y.Jiang, Z.Cong, Y.Feng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.43 / 1.56
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.505, 147.013, 64.541, 90, 99.96, 90
R / Rfree (%) 16.8 / 19.8

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87V/T268V/A184V in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine and Hydroxylamine (pdb code 7yda). 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 the P450 BM3 Heme Domain Mutant F87V/T268V/A184V in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine and Hydroxylamine, PDB code: 7yda:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 7yda

Go back to Iron Binding Sites List in 7yda
Iron binding site 1 out of 2 in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87V/T268V/A184V in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine and Hydroxylamine


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 the P450 BM3 Heme Domain Mutant F87V/T268V/A184V in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine and Hydroxylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:15.8
occ:1.00
 FE A:HEM501 0.0 15.8 1.0
NB A:HEM501 2.0 16.6 1.0
NC A:HEM501 2.0 12.8 1.0
NA A:HEM501 2.0 14.7 1.0
ND A:HEM501 2.0 16.2 1.0
SG A:CYS400 2.3 15.3 1.0
N A:HOA503 2.4 23.0 1.0
HN1 A:HOA503 2.8 27.6 1.0
O A:HOA503 2.8 29.7 1.0
HN2 A:HOA503 3.0 27.6 1.0
C1B A:HEM501 3.0 16.8 1.0
C1C A:HEM501 3.0 16.2 1.0
C4B A:HEM501 3.0 17.4 1.0
C1D A:HEM501 3.0 18.5 1.0
C4A A:HEM501 3.1 15.5 1.0
C4C A:HEM501 3.1 14.8 1.0
C1A A:HEM501 3.1 16.6 1.0
C4D A:HEM501 3.1 15.9 1.0
HO A:HOA503 3.2 35.6 1.0
CB A:CYS400 3.3 13.5 1.0
CHC A:HEM501 3.5 16.6 1.0
CHD A:HEM501 3.5 18.1 1.0
CHA A:HEM501 3.5 17.1 1.0
CHB A:HEM501 3.5 15.9 1.0
CA A:CYS400 4.0 14.2 1.0
C3B A:HEM501 4.2 16.0 1.0
C2B A:HEM501 4.2 13.3 1.0
C2D A:HEM501 4.2 16.3 1.0
C3C A:HEM501 4.3 16.2 1.0
C2C A:HEM501 4.3 17.4 1.0
C3A A:HEM501 4.3 13.9 1.0
C2A A:HEM501 4.3 15.3 1.0
C3D A:HEM501 4.3 16.1 1.0
N A:GLY402 4.8 15.4 1.0
CB A:ALA264 4.8 22.4 1.0
C A:CYS400 4.8 16.6 1.0
N A:ILE401 5.0 16.9 1.0

Iron binding site 2 out of 2 in 7yda

Go back to Iron Binding Sites List in 7yda
Iron binding site 2 out of 2 in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87V/T268V/A184V in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine and Hydroxylamine


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 the P450 BM3 Heme Domain Mutant F87V/T268V/A184V in Complex with N-Imidazolyl-Pentanoyl-L-Phenylalanine and Hydroxylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:16.2
occ:1.00
 FE B:HEM501 0.0 16.2 1.0
ND B:HEM501 2.0 16.2 1.0
NB B:HEM501 2.0 17.2 1.0
NA B:HEM501 2.0 16.2 1.0
NC B:HEM501 2.0 15.1 1.0
N B:HOA503 2.2 20.2 1.0
HN2 B:HOA503 2.2 24.2 1.0
SG B:CYS400 2.3 16.5 1.0
HN1 B:HOA503 2.8 24.2 1.0
C1B B:HEM501 3.0 15.4 1.0
C1D B:HEM501 3.0 15.9 1.0
C4D B:HEM501 3.0 18.3 1.0
C4C B:HEM501 3.0 16.6 1.0
C4A B:HEM501 3.0 16.0 1.0
C4B B:HEM501 3.0 17.0 1.0
C1A B:HEM501 3.1 16.1 1.0
C1C B:HEM501 3.1 16.1 1.0
O B:HOA503 3.1 31.6 1.0
CB B:CYS400 3.3 14.7 1.0
CHB B:HEM501 3.4 15.8 1.0
CHA B:HEM501 3.4 15.5 1.0
CHD B:HEM501 3.5 18.0 1.0
CHC B:HEM501 3.5 17.1 1.0
HO B:HOA503 3.9 37.9 1.0
CA B:CYS400 4.0 15.9 1.0
C3D B:HEM501 4.2 16.3 1.0
C2D B:HEM501 4.2 18.1 1.0
C2B B:HEM501 4.2 15.6 1.0
C3B B:HEM501 4.2 17.7 1.0
C3C B:HEM501 4.2 19.3 1.0
C3A B:HEM501 4.3 16.0 1.0
C2A B:HEM501 4.3 14.7 1.0
C2C B:HEM501 4.3 19.3 1.0
C B:CYS400 4.8 17.4 1.0
CB B:ALA264 4.8 24.4 1.0
N B:GLY402 4.9 16.3 1.0
N B:ILE401 5.0 16.2 1.0

Reference:

J.Chen, S.Dong, W.Fang, Y.Jiang, Z.Chen, X.Qin, C.Wang, H.Zhou, L.Jin, Y.Feng, B.Wang, Z.Cong. Regiodivergent and Enantioselective Hydroxylation of C-H Bonds By Synergistic Use of Protein Engineering and Exogenous Dual-Functional Small Molecules. Angew.Chem.Int.Ed.Engl. V. 62 15088 2023.
ISSN: ESSN 1521-3773
PubMed: 36417593
DOI: 10.1002/ANIE.202215088
Page generated: Fri Aug 9 12:15:50 2024

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