Atomistry » Manganese » PDB 2dvd-2fer » 2fe6
Atomistry »
  Manganese »
    PDB 2dvd-2fer »
      2fe6 »

Manganese in PDB 2fe6: P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX

Enzymatic activity of P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX

All present enzymatic activity of P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX:
1.14.15.1;

Protein crystallography data

The structure of P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX, PDB code: 2fe6 was solved by K.Von Koenig, T.M.Makris, S.G.Sligar, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.00 / 1.50
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 64.390, 64.390, 252.730, 90.00, 90.00, 90.00
R / Rfree (%) 22.7 / 24.9

Other elements in 2fe6:

The structure of P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX also contains other interesting chemical elements:

Potassium (K) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX (pdb code 2fe6). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX, PDB code: 2fe6:

Manganese binding site 1 out of 1 in 2fe6

Go back to Manganese Binding Sites List in 2fe6
Manganese binding site 1 out of 1 in the P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of P450CAM From Pseudomonas Putida Reconstituted with Manganic Protoporphyrin IX within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn422

b:7.0
occ:1.00
 MN A:MNR422 0.0 7.0 1.0
NA A:MNR422 2.0 8.3 1.0
NB A:MNR422 2.0 7.4 1.0
NC A:MNR422 2.0 10.0 1.0
ND A:MNR422 2.1 5.8 1.0
SG A:CYS357 2.6 6.4 1.0
O A:HOH852 2.9 26.8 1.0
C1C A:MNR422 3.1 9.7 1.0
C4B A:MNR422 3.1 9.8 1.0
C1A A:MNR422 3.1 8.4 1.0
C4A A:MNR422 3.1 8.6 1.0
C1B A:MNR422 3.1 10.8 1.0
C4C A:MNR422 3.1 9.6 1.0
C4D A:MNR422 3.1 7.8 1.0
C1D A:MNR422 3.1 7.5 1.0
CHC A:MNR422 3.4 10.4 1.0
CHB A:MNR422 3.5 8.9 1.0
CHA A:MNR422 3.5 8.5 1.0
CHD A:MNR422 3.5 8.6 1.0
CB A:CYS357 3.5 9.6 1.0
CA A:CYS357 4.1 9.4 1.0
C3A A:MNR422 4.3 7.9 1.0
C2C A:MNR422 4.3 9.3 1.0
C3C A:MNR422 4.3 11.2 1.0
C2A A:MNR422 4.3 9.1 1.0
C2B A:MNR422 4.4 13.0 1.0
C3D A:MNR422 4.4 8.0 1.0
C2D A:MNR422 4.4 7.5 1.0
C3B A:MNR422 4.4 11.1 1.0
O A:HOH850 4.4 26.6 1.0
N A:GLY359 4.5 9.1 1.0
N A:LEU358 4.7 8.8 1.0
C A:CYS357 4.8 9.4 1.0
CA A:GLY359 4.9 10.6 1.0
O A:HOH851 4.9 25.6 1.0

Reference:

T.M.Makris, K.Koenig, I.Schlichting, S.G.Sligar. The Status of High-Valent Metal Oxo Complexes in the P450 Cytochromes. J.Inorg.Biochem. V. 100 507 2006.
ISSN: ISSN 0162-0134
PubMed: 16510191
DOI: 10.1016/J.JINORGBIO.2006.01.025
Page generated: Sat Oct 5 14:05:14 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy