Atomistry » Iron » PDB 7oqy-7p7j » 7p6l
Atomistry »
  Iron »
    PDB 7oqy-7p7j »
      7p6l »

Iron in PDB 7p6l: Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid

Enzymatic activity of Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid

All present enzymatic activity of Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid:
1.14.14.1; 1.6.2.4;

Protein crystallography data

The structure of Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid, PDB code: 7p6l was solved by D.J.Opperman, J.C.Aschenbrenner, C.Tolmie, A.C.Ebrecht, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 61.43 / 2.33
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 171.49, 171.49, 175.647, 90, 90, 90
R / Rfree (%) 20.3 / 23.4

Iron Binding Sites:

The binding sites of Iron atom in the Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid (pdb code 7p6l). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid, PDB code: 7p6l:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 7p6l

Go back to Iron Binding Sites List in 7p6l
Iron binding site 1 out of 4 in the Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:79.3
occ:1.00
FE B:HEM501 0.0 79.3 1.0
ND B:HEM501 1.9 84.6 1.0
NA B:HEM501 2.0 79.2 1.0
NB B:HEM501 2.1 82.0 1.0
NC B:HEM501 2.1 84.1 1.0
SG B:CYS411 2.3 78.6 1.0
O B:HOH610 2.8 76.6 1.0
C4D B:HEM501 2.9 79.2 1.0
C1D B:HEM501 2.9 80.9 1.0
C1A B:HEM501 3.0 78.2 1.0
C4B B:HEM501 3.1 76.8 1.0
C1B B:HEM501 3.1 80.3 1.0
C4C B:HEM501 3.1 82.5 1.0
C4A B:HEM501 3.1 77.6 1.0
C1C B:HEM501 3.1 80.0 1.0
CHA B:HEM501 3.3 78.4 1.0
CB B:CYS411 3.4 80.5 1.0
CHD B:HEM501 3.4 81.0 1.0
CHC B:HEM501 3.5 75.9 1.0
CHB B:HEM501 3.5 80.8 1.0
CA B:CYS411 4.1 80.2 1.0
C3D B:HEM501 4.2 80.9 1.0
C2D B:HEM501 4.2 80.2 1.0
C2A B:HEM501 4.2 77.9 1.0
C3A B:HEM501 4.2 77.8 1.0
C2B B:HEM501 4.3 69.8 1.0
C2C B:HEM501 4.3 79.6 1.0
C3C B:HEM501 4.3 79.2 1.0
C3B B:HEM501 4.3 77.5 1.0
O B:ALA270 4.5 71.6 1.0
CE2 B:PHE93 4.8 79.6 1.0
OG1 B:THR274 4.9 68.3 1.0
C B:CYS411 5.0 76.7 1.0
N B:GLY413 5.0 75.5 1.0
CB B:ALA270 5.0 71.7 1.0

Iron binding site 2 out of 4 in 7p6l

Go back to Iron Binding Sites List in 7p6l
Iron binding site 2 out of 4 in the Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:68.9
occ:1.00
FE A:HEM501 0.0 68.9 1.0
ND A:HEM501 1.9 65.3 1.0
NB A:HEM501 2.0 62.6 1.0
NA A:HEM501 2.1 66.3 1.0
NC A:HEM501 2.1 63.2 1.0
SG A:CYS411 2.3 75.3 1.0
C4D A:HEM501 2.9 63.6 1.0
C1D A:HEM501 3.0 64.3 1.0
C4B A:HEM501 3.0 62.8 1.0
C1B A:HEM501 3.0 66.9 1.0
C1A A:HEM501 3.1 65.8 1.0
C1C A:HEM501 3.1 64.7 1.0
C4A A:HEM501 3.1 67.4 1.0
C4C A:HEM501 3.1 62.8 1.0
CB A:CYS411 3.2 72.4 1.0
O A:HOH605 3.3 58.7 1.0
CHC A:HEM501 3.4 62.7 1.0
CHA A:HEM501 3.4 65.7 1.0
CHB A:HEM501 3.5 68.6 1.0
CHD A:HEM501 3.5 64.1 1.0
CA A:CYS411 4.0 73.8 1.0
C3D A:HEM501 4.2 62.2 1.0
C2D A:HEM501 4.2 62.5 1.0
C2B A:HEM501 4.3 68.4 1.0
C3B A:HEM501 4.3 66.3 1.0
C2A A:HEM501 4.3 66.6 1.0
C3A A:HEM501 4.3 67.6 1.0
C2C A:HEM501 4.3 65.9 1.0
C3C A:HEM501 4.3 62.3 1.0
O A:ALA270 4.6 69.0 1.0
C A:CYS411 4.8 72.2 1.0
N A:GLY413 4.8 69.3 1.0
CE2 A:PHE93 4.9 65.7 1.0
OG1 A:THR274 4.9 58.9 1.0
N A:ILE412 5.0 71.8 1.0

Iron binding site 3 out of 4 in 7p6l

Go back to Iron Binding Sites List in 7p6l
Iron binding site 3 out of 4 in the Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:73.2
occ:1.00
FE C:HEM501 0.0 73.2 1.0
ND C:HEM501 1.9 74.6 1.0
NA C:HEM501 2.0 74.8 1.0
NB C:HEM501 2.1 67.9 1.0
NC C:HEM501 2.1 73.4 1.0
SG C:CYS411 2.3 74.7 1.0
C4D C:HEM501 2.9 74.9 1.0
C1D C:HEM501 3.0 72.7 1.0
O C:HOH626 3.0 73.8 1.0
C1A C:HEM501 3.0 74.2 1.0
C4B C:HEM501 3.0 67.1 1.0
C1B C:HEM501 3.1 69.7 1.0
C4A C:HEM501 3.1 72.0 1.0
C4C C:HEM501 3.1 71.1 1.0
C1C C:HEM501 3.1 68.2 1.0
CB C:CYS411 3.2 71.9 1.0
CHA C:HEM501 3.4 75.3 1.0
CHC C:HEM501 3.5 67.3 1.0
CHB C:HEM501 3.5 70.1 1.0
CHD C:HEM501 3.5 72.0 1.0
CA C:CYS411 3.9 74.8 1.0
C3D C:HEM501 4.2 70.1 1.0
C2D C:HEM501 4.2 71.9 1.0
C2A C:HEM501 4.2 71.3 1.0
C3A C:HEM501 4.3 70.8 1.0
C3B C:HEM501 4.3 66.3 1.0
C2B C:HEM501 4.3 68.0 1.0
C2C C:HEM501 4.3 68.8 1.0
C3C C:HEM501 4.4 70.3 1.0
O C:ALA270 4.6 78.0 1.0
C C:CYS411 4.8 74.6 1.0
CE2 C:PHE93 4.8 81.0 1.0
N C:GLY413 4.9 68.9 1.0
OG1 C:THR274 4.9 74.9 1.0
CB C:ALA270 4.9 74.2 1.0

Iron binding site 4 out of 4 in 7p6l

Go back to Iron Binding Sites List in 7p6l
Iron binding site 4 out of 4 in the Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Heme Domain of CYP505A30, A Fungal Hydroxylase From Myceliophthora Thermophila, Bound to Dodecanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:78.4
occ:1.00
FE D:HEM501 0.0 78.4 1.0
ND D:HEM501 1.9 81.8 1.0
NA D:HEM501 2.0 87.8 1.0
NB D:HEM501 2.1 81.4 1.0
NC D:HEM501 2.1 82.5 1.0
SG D:CYS411 2.2 73.1 1.0
O D:HOH607 2.9 70.1 1.0
C1D D:HEM501 2.9 77.6 1.0
C4D D:HEM501 3.0 78.6 1.0
C1A D:HEM501 3.0 86.3 1.0
C1B D:HEM501 3.1 86.1 1.0
C4C D:HEM501 3.1 76.1 1.0
C4B D:HEM501 3.1 83.8 1.0
C4A D:HEM501 3.1 83.1 1.0
C1C D:HEM501 3.2 83.3 1.0
CB D:CYS411 3.2 79.9 1.0
CHA D:HEM501 3.3 85.4 1.0
CHD D:HEM501 3.4 74.0 1.0
CHB D:HEM501 3.5 84.9 1.0
CHC D:HEM501 3.5 86.1 1.0
CA D:CYS411 3.9 81.1 1.0
C2D D:HEM501 4.2 76.1 1.0
C3D D:HEM501 4.2 75.4 1.0
C2A D:HEM501 4.3 83.8 1.0
C2B D:HEM501 4.3 84.7 1.0
C3A D:HEM501 4.3 86.3 1.0
C3C D:HEM501 4.3 84.4 1.0
C3B D:HEM501 4.3 81.7 1.0
C2C D:HEM501 4.3 85.7 1.0
O D:ALA270 4.6 64.0 1.0
C D:CYS411 4.7 84.9 1.0
N D:GLY413 4.8 76.7 1.0
CE2 D:PHE93 4.9 77.0 1.0
N D:ILE412 4.9 81.5 1.0
OG1 D:THR274 5.0 66.8 1.0

Reference:

J.C.Aschenbrenner, A.C.Ebrecht, C.Tolmie, M.S.Smit, D.J.Opperman. Structure of the Fungal Hydroxylase, CYP505A30, and Rational Transfer of Mutation Data From CYP102A1 to Alter Regioselectivity Catalysis Science and V. 11 7359 2021TECHNOLOGY.
ISSN: ESSN 2044-4761
DOI: 10.1039/D1CY01348C
Page generated: Thu Aug 8 15:04:25 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy