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Iron in PDB 4l4d: Structure of Cyanide and Camphor Bound P450CAM Mutant L358A

Enzymatic activity of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A

All present enzymatic activity of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A:
1.14.15.1;

Protein crystallography data

The structure of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A, PDB code: 4l4d was solved by D.Batabyal, H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.52 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.614, 103.586, 105.733, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 24

Other elements in 4l4d:

The structure of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A also contains other interesting chemical elements:

Potassium (K) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358A (pdb code 4l4d). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358A, PDB code: 4l4d:

Iron binding site 1 out of 1 in 4l4d

Go back to Iron Binding Sites List in 4l4d
Iron binding site 1 out of 1 in the Structure of Cyanide and Camphor Bound P450CAM Mutant L358A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Cyanide and Camphor Bound P450CAM Mutant L358A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:16.4
occ:1.00
FE A:HEM501 0.0 16.4 1.0
C A:CYN502 2.1 17.3 1.0
NB A:HEM501 2.2 11.0 1.0
NC A:HEM501 2.2 13.3 1.0
ND A:HEM501 2.2 14.0 1.0
NA A:HEM501 2.2 12.8 1.0
SG A:CYS357 2.3 7.8 1.0
N A:CYN502 3.1 18.9 1.0
C1D A:HEM501 3.1 15.2 1.0
C4C A:HEM501 3.1 19.6 1.0
C1B A:HEM501 3.1 9.0 1.0
C4B A:HEM501 3.2 9.4 1.0
C4A A:HEM501 3.2 8.3 1.0
C1C A:HEM501 3.2 11.6 1.0
C4D A:HEM501 3.2 16.5 1.0
C1A A:HEM501 3.2 11.6 1.0
CB A:CYS357 3.3 10.7 1.0
CHD A:HEM501 3.4 18.3 1.0
CHB A:HEM501 3.5 4.9 1.0
CHC A:HEM501 3.5 12.7 1.0
CHA A:HEM501 3.5 10.6 1.0
CA A:CYS357 4.2 10.8 1.0
C2D A:HEM501 4.4 14.7 1.0
C3C A:HEM501 4.4 20.7 1.0
C2B A:HEM501 4.4 5.5 1.0
C3B A:HEM501 4.4 4.2 1.0
C2C A:HEM501 4.4 13.1 1.0
C3D A:HEM501 4.4 18.2 1.0
C3A A:HEM501 4.4 10.2 1.0
C2A A:HEM501 4.4 14.4 1.0
C5 A:CAM503 4.5 18.7 1.0
N A:GLY359 4.7 13.8 1.0
OG1 A:THR252 4.8 14.5 1.0
C A:CYS357 4.9 11.1 1.0
N A:ALA358 4.9 14.6 1.0
C9 A:CAM503 5.0 10.7 1.0

Reference:

D.Batabyal, H.Li, T.L.Poulos. Synergistic Effects of Mutations in Cytochrome P450CAM Designed to Mimic CYP101D1. Biochemistry V. 52 5396 2013.
ISSN: ISSN 0006-2960
PubMed: 23865948
DOI: 10.1021/BI400676D
Page generated: Mon Aug 5 06:08:45 2024

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