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Potassium in PDB 6fsh: Crystal Structure of Hybrid P450 Oxybtei(Bc/Fgvan)

Protein crystallography data

The structure of Crystal Structure of Hybrid P450 Oxybtei(Bc/Fgvan), PDB code: 6fsh was solved by C.Brieke, M.Tarnawski, A.Greule, M.J.Cryle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.26 / 2.50
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 59.270, 83.160, 92.220, 85.20, 101.98, 97.83
R / Rfree (%) 18.8 / 24.6

Other elements in 6fsh:

The structure of Crystal Structure of Hybrid P450 Oxybtei(Bc/Fgvan) also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Hybrid P450 Oxybtei(Bc/Fgvan) (pdb code 6fsh). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Crystal Structure of Hybrid P450 Oxybtei(Bc/Fgvan), PDB code: 6fsh:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in 6fsh

Go back to Potassium Binding Sites List in 6fsh
Potassium binding site 1 out of 3 in the Crystal Structure of Hybrid P450 Oxybtei(Bc/Fgvan)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Hybrid P450 Oxybtei(Bc/Fgvan) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K402

b:67.1
occ:1.00
OH A:TYR284 2.6 47.8 1.0
C A:THR384 2.9 58.1 1.0
CA A:THR384 3.0 44.0 1.0
O A:ARG383 3.0 53.8 1.0
O A:THR386 3.1 57.6 1.0
O A:THR384 3.2 60.1 1.0
N A:THR386 3.2 67.6 1.0
N A:SER385 3.3 65.2 1.0
OG1 A:THR386 3.4 65.3 1.0
N A:THR384 3.4 43.0 1.0
C A:ARG383 3.5 42.7 1.0
CZ A:TYR284 3.5 34.2 1.0
CE2 A:TYR284 3.6 40.8 1.0
O A:ALA388 3.6 42.1 1.0
C A:THR386 3.8 59.3 1.0
C A:ALA388 3.9 36.2 1.0
CA A:THR386 4.0 63.6 1.0
C A:SER385 4.0 71.7 1.0
CA A:TYR389 4.0 32.8 1.0
N A:TYR389 4.0 32.8 1.0
CA A:SER385 4.2 75.3 1.0
CB A:THR386 4.3 68.2 1.0
CB A:THR384 4.4 41.8 1.0
N A:ALA388 4.5 41.9 1.0
CD1 A:TYR389 4.6 43.2 1.0
CA A:ARG383 4.7 49.5 1.0
CB A:ARG383 4.8 44.4 1.0
CE1 A:TYR284 4.8 32.3 1.0
CA A:ALA388 4.8 38.5 1.0
CD2 A:TYR284 4.9 45.0 1.0
N A:PRO387 4.9 48.1 1.0
CG A:ARG383 5.0 43.6 1.0
C A:TYR389 5.0 34.1 1.0

Potassium binding site 2 out of 3 in 6fsh

Go back to Potassium Binding Sites List in 6fsh
Potassium binding site 2 out of 3 in the Crystal Structure of Hybrid P450 Oxybtei(Bc/Fgvan)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Hybrid P450 Oxybtei(Bc/Fgvan) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K403

b:0.5
occ:1.00
O A:LEU235 3.2 50.2 1.0
N A:ASP239 3.2 50.3 1.0
CB A:ASP239 3.2 56.5 1.0
CB A:ASP238 3.6 67.0 1.0
CA A:ASP239 3.8 44.2 1.0
O A:HOH518 3.9 41.3 1.0
C A:LEU235 4.0 45.3 1.0
CA A:LEU235 4.1 50.3 1.0
C A:ASP238 4.2 47.0 1.0
CA A:ASP238 4.3 55.3 1.0
CG A:ASP239 4.3 78.7 1.0
N A:ASP238 4.4 55.9 1.0
O A:MET234 4.4 53.0 1.0
OD1 A:ASP239 4.4 85.9 1.0
CG A:ASP238 4.6 81.5 1.0
CB A:LEU235 4.9 58.5 1.0

Potassium binding site 3 out of 3 in 6fsh

Go back to Potassium Binding Sites List in 6fsh
Potassium binding site 3 out of 3 in the Crystal Structure of Hybrid P450 Oxybtei(Bc/Fgvan)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of Hybrid P450 Oxybtei(Bc/Fgvan) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K402

b:87.8
occ:1.00
ND1 B:HIS346 2.9 39.6 1.0
O B:CYS347 3.1 27.8 1.0
NH2 B:ARG100 3.3 31.6 1.0
CE1 B:HIS346 3.7 29.1 1.0
O B:HIS346 3.8 37.7 1.0
C B:CYS347 3.9 30.7 1.0
CG B:HIS346 4.0 38.0 1.0
CA B:LEU348 4.1 36.9 1.0
C B:HIS346 4.3 40.4 1.0
CB B:HIS346 4.3 28.7 1.0
N B:LEU348 4.4 34.1 1.0
CD1 B:LEU348 4.5 48.4 1.0
CZ B:ARG100 4.6 41.7 1.0
O B:LEU348 4.6 29.0 1.0
C B:LEU348 4.6 42.1 1.0
N B:CYS347 4.8 28.6 1.0
CB B:ALA350 4.9 27.1 1.0
NE2 B:HIS346 4.9 32.1 1.0
CA B:HIS346 5.0 40.4 1.0
CA B:CYS347 5.0 27.2 1.0

Reference:

C.Brieke, M.Tarnawski, A.Greule, M.J.Cryle. Investigating Cytochrome P450 Specificity During Glycopeptide Antibiotic Biosynthesis Through A Homologue Hybridization Approach. J. Inorg. Biochem. V. 185 43 2018.
ISSN: ISSN 1873-3344
PubMed: 29751197
DOI: 10.1016/J.JINORGBIO.2018.05.001
Page generated: Mon Aug 12 16:07:29 2024

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