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Manganese in PDB 2fer: 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: 2fer 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) 17.59 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.320, 63.820, 105.440, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 22.5

Other elements in 2fer:

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 2fer). 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: 2fer:

Manganese binding site 1 out of 1 in 2fer

Go back to Manganese Binding Sites List in 2fer
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:Mn1001

b:13.3
occ:1.00
 MN A:MNR1001 0.0 13.3 1.0
NC A:MNR1001 2.0 13.8 1.0
NA A:MNR1001 2.1 13.5 1.0
ND A:MNR1001 2.1 12.7 1.0
NB A:MNR1001 2.1 12.9 1.0
SG A:CYS357 2.5 14.7 1.0
O A:HOH1392 2.7 27.0 0.5
C1C A:MNR1001 3.0 13.1 1.0
C4C A:MNR1001 3.1 12.6 1.0
C1D A:MNR1001 3.1 13.7 1.0
C4A A:MNR1001 3.1 11.9 1.0
C4B A:MNR1001 3.1 13.6 1.0
C1A A:MNR1001 3.1 12.0 1.0
C4D A:MNR1001 3.1 12.3 1.0
C1B A:MNR1001 3.1 12.3 1.0
CHC A:MNR1001 3.4 12.1 1.0
CB A:CYS357 3.4 15.2 1.0
CHD A:MNR1001 3.4 14.8 1.0
CHB A:MNR1001 3.5 12.3 1.0
CHA A:MNR1001 3.5 11.5 1.0
CA A:CYS357 4.1 14.1 1.0
C2C A:MNR1001 4.3 13.9 1.0
C3C A:MNR1001 4.3 13.4 1.0
C3A A:MNR1001 4.3 11.2 1.0
C2A A:MNR1001 4.3 12.7 1.0
C2D A:MNR1001 4.3 12.7 1.0
C3B A:MNR1001 4.3 12.5 1.0
O A:HOH1392 4.3 37.5 0.5
C2B A:MNR1001 4.3 13.0 1.0
C3D A:MNR1001 4.3 12.5 1.0
N A:GLY359 4.5 14.5 1.0
N A:LEU358 4.8 14.2 1.0
C A:CYS357 4.8 15.0 1.0
CA A:GLY359 4.9 12.7 1.0
O A:HOH1413 5.0 47.3 1.0

Reference:

T.M.Makris, K.Von 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 Aug 16 10:12:02 2025

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