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Iron in PDB 7yft: Crystal Structure of the P450 BM3 Heme Domain Mutant F87A/T268V/A82C/L181M in Complex with N-Imidazolyl-Pentanoyl-L- Phenylalanine, Indane and Hydroxylamine

Enzymatic activity of Crystal Structure of the P450 BM3 Heme Domain Mutant F87A/T268V/A82C/L181M in Complex with N-Imidazolyl-Pentanoyl-L- Phenylalanine, Indane and Hydroxylamine

All present enzymatic activity of Crystal Structure of the P450 BM3 Heme Domain Mutant F87A/T268V/A82C/L181M in Complex with N-Imidazolyl-Pentanoyl-L- Phenylalanine, Indane 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 F87A/T268V/A82C/L181M in Complex with N-Imidazolyl-Pentanoyl-L- Phenylalanine, Indane and Hydroxylamine, PDB code: 7yft 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) 38.48 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 56.93, 143.73, 62.44, 90, 100.01, 90
R / Rfree (%) 24.1 / 26.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A/T268V/A82C/L181M in Complex with N-Imidazolyl-Pentanoyl-L- Phenylalanine, Indane and Hydroxylamine (pdb code 7yft). 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 F87A/T268V/A82C/L181M in Complex with N-Imidazolyl-Pentanoyl-L- Phenylalanine, Indane and Hydroxylamine, PDB code: 7yft:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 7yft

Go back to Iron Binding Sites List in 7yft
Iron binding site 1 out of 2 in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A/T268V/A82C/L181M in Complex with N-Imidazolyl-Pentanoyl-L- Phenylalanine, Indane 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 F87A/T268V/A82C/L181M in Complex with N-Imidazolyl-Pentanoyl-L- Phenylalanine, Indane and Hydroxylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:15.9
occ:1.00
 FE A:HEM501 0.0 15.9 1.0
ND A:HEM501 1.9 16.0 1.0
NA A:HEM501 2.0 15.7 1.0
NC A:HEM501 2.1 18.9 1.0
NB A:HEM501 2.1 21.7 1.0
HN2 A:HOA502 2.5 40.7 1.0
SG A:CYS400 2.5 18.8 1.0
N A:HOA502 2.6 33.9 1.0
HB2 A:CYS400 2.7 25.1 1.0
C4D A:HEM501 2.8 14.1 1.0
HN1 A:HOA502 2.9 40.7 1.0
C1D A:HEM501 2.9 16.1 1.0
C1A A:HEM501 2.9 10.6 1.0
C4C A:HEM501 3.0 21.6 1.0
C4A A:HEM501 3.0 16.4 1.0
CB A:CYS400 3.1 20.9 1.0
C1B A:HEM501 3.1 21.4 1.0
C4B A:HEM501 3.1 20.9 1.0
C1C A:HEM501 3.1 22.0 1.0
CHA A:HEM501 3.3 9.5 1.0
CHD A:HEM501 3.3 17.0 1.0
CHB A:HEM501 3.5 19.0 1.0
CHC A:HEM501 3.5 20.4 1.0
HA A:CYS400 3.5 20.9 1.0
HB1 A:ALA264 3.7 35.6 1.0
HB3 A:CYS400 3.9 25.1 1.0
CA A:CYS400 3.9 17.4 1.0
O A:HOA502 3.9 34.7 1.0
HO A:HOA502 4.1 41.6 1.0
C3D A:HEM501 4.1 14.1 1.0
HD1 A:PHE393 4.1 17.2 1.0
C2D A:HEM501 4.1 14.4 1.0
H A:GLY402 4.1 17.1 1.0
C2A A:HEM501 4.1 12.6 1.0
C3A A:HEM501 4.2 14.0 1.0
C3C A:HEM501 4.3 29.7 1.0
C2B A:HEM501 4.3 19.7 1.0
C2C A:HEM501 4.3 27.9 1.0
C3B A:HEM501 4.3 19.9 1.0
HG11 A:VAL268 4.5 26.9 1.0
CB A:ALA264 4.6 29.7 1.0
C A:CYS400 4.7 14.7 1.0
HB2 A:ALA264 4.8 35.6 1.0
H A:ILE401 4.8 16.1 1.0
HA3 A:GLY402 4.8 18.5 1.0
N A:GLY402 4.9 14.2 1.0
N A:CYS400 5.0 16.0 1.0
CD1 A:PHE393 5.0 14.3 1.0
N A:ILE401 5.0 13.4 1.0

Iron binding site 2 out of 2 in 7yft

Go back to Iron Binding Sites List in 7yft
Iron binding site 2 out of 2 in the Crystal Structure of the P450 BM3 Heme Domain Mutant F87A/T268V/A82C/L181M in Complex with N-Imidazolyl-Pentanoyl-L- Phenylalanine, Indane 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 F87A/T268V/A82C/L181M in Complex with N-Imidazolyl-Pentanoyl-L- Phenylalanine, Indane and Hydroxylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:14.7
occ:1.00
 FE B:HEM502 0.0 14.7 1.0
ND B:HEM502 1.9 12.8 1.0
NA B:HEM502 2.0 12.5 1.0
NC B:HEM502 2.1 10.8 1.0
NB B:HEM502 2.1 12.6 1.0
SG B:CYS400 2.3 14.8 1.0
HN1 B:HOA501 2.3 33.4 1.0
N B:HOA501 2.5 27.9 1.0
C4D B:HEM502 2.9 13.8 1.0
C1D B:HEM502 2.9 12.3 1.0
C1A B:HEM502 2.9 13.9 1.0
C4A B:HEM502 3.0 13.1 1.0
C4C B:HEM502 3.0 11.8 1.0
C1B B:HEM502 3.1 14.1 1.0
C4B B:HEM502 3.1 13.6 1.0
HB2 B:CYS400 3.1 20.6 1.0
C1C B:HEM502 3.1 12.1 1.0
HN2 B:HOA501 3.2 33.4 1.0
HO B:HOA501 3.2 35.8 1.0
CB B:CYS400 3.3 17.2 1.0
CHA B:HEM502 3.3 12.8 1.0
CHD B:HEM502 3.3 11.4 1.0
O B:HOA501 3.4 29.8 1.0
CHB B:HEM502 3.4 14.1 1.0
CHC B:HEM502 3.5 13.0 1.0
HA B:CYS400 3.6 18.7 1.0
HB1 B:ALA264 3.9 33.7 1.0
CA B:CYS400 4.0 15.6 1.0
HB3 B:CYS400 4.1 20.6 1.0
C3D B:HEM502 4.1 14.3 1.0
C2D B:HEM502 4.1 13.7 1.0
C2A B:HEM502 4.1 14.2 1.0
H B:GLY402 4.1 18.6 1.0
C3A B:HEM502 4.2 12.4 1.0
C3C B:HEM502 4.3 12.8 1.0
HD1 B:PHE393 4.3 17.2 1.0
C2C B:HEM502 4.3 12.9 1.0
C2B B:HEM502 4.3 13.3 1.0
C3B B:HEM502 4.3 13.7 1.0
H3 B:16N503 4.4 97.0 1.0
HB2 B:ALA264 4.6 33.7 1.0
H18 B:IRV504 4.6 82.2 0.5
CB B:ALA264 4.7 28.1 1.0
HG11 B:VAL268 4.7 24.5 1.0
HA3 B:GLY402 4.8 21.0 1.0
C B:CYS400 4.8 14.0 1.0
N22 B:IRV504 4.9 69.2 0.5
H B:ILE401 4.9 17.3 1.0
N B:GLY402 4.9 15.5 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 12:19:17 2024

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