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Iron in PDB 2l8m: Reduced and Co-Bound Cytochrome P450CAM (CYP101A1)

Enzymatic activity of Reduced and Co-Bound Cytochrome P450CAM (CYP101A1)

All present enzymatic activity of Reduced and Co-Bound Cytochrome P450CAM (CYP101A1):
1.14.15.1;

Other elements in 2l8m:

The structure of Reduced and Co-Bound Cytochrome P450CAM (CYP101A1) also contains other interesting chemical elements:

Potassium (K) 4 atoms
Chlorine (Cl) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Reduced and Co-Bound Cytochrome P450CAM (CYP101A1) (pdb code 2l8m). 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 Reduced and Co-Bound Cytochrome P450CAM (CYP101A1), PDB code: 2l8m:

Iron binding site 1 out of 1 in 2l8m

Go back to Iron Binding Sites List in 2l8m
Iron binding site 1 out of 1 in the Reduced and Co-Bound Cytochrome P450CAM (CYP101A1)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Reduced and Co-Bound Cytochrome P450CAM (CYP101A1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe416

b:0.0
occ:1.00
FE A:HEM416 0.0 0.0 1.0
C A:CMO417 1.8 0.0 1.0
NA A:HEM416 1.9 0.0 1.0
ND A:HEM416 2.0 0.0 1.0
NB A:HEM416 2.0 0.0 1.0
NC A:HEM416 2.1 0.0 1.0
SG A:CYS357 2.5 0.0 1.0
O A:CMO417 2.9 0.0 1.0
C1A A:HEM416 2.9 0.0 1.0
C4D A:HEM416 3.0 0.0 1.0
C4A A:HEM416 3.0 0.0 1.0
C1B A:HEM416 3.0 0.0 1.0
C1D A:HEM416 3.1 0.0 1.0
C4B A:HEM416 3.1 0.0 1.0
C4C A:HEM416 3.1 0.0 1.0
C1C A:HEM416 3.1 0.0 1.0
CHA A:HEM416 3.3 0.0 1.0
HE21 A:GLN360 3.3 0.0 1.0
HB2 A:CYS357 3.3 0.0 1.0
CHB A:HEM416 3.4 0.0 1.0
CHC A:HEM416 3.5 0.0 1.0
CHD A:HEM416 3.5 0.0 1.0
CB A:CYS357 3.5 0.0 1.0
HB3 A:GLN360 3.5 0.0 1.0
HA A:CYS357 3.6 0.0 1.0
H A:GLN360 3.7 0.0 1.0
H A:GLY359 3.8 0.0 1.0
CA A:CYS357 4.1 0.0 1.0
H A:LEU358 4.2 0.0 1.0
C2A A:HEM416 4.2 0.0 1.0
NE2 A:GLN360 4.2 0.0 1.0
C3D A:HEM416 4.2 0.0 1.0
C3A A:HEM416 4.2 0.0 1.0
C2B A:HEM416 4.3 0.0 1.0
H93 A:CAM415 4.3 0.0 1.0
C3B A:HEM416 4.3 0.0 1.0
C2C A:HEM416 4.3 0.0 1.0
C2D A:HEM416 4.3 0.0 1.0
C3C A:HEM416 4.3 0.0 1.0
HHA A:HEM416 4.4 0.0 1.0
HB3 A:CYS357 4.4 0.0 1.0
HG1 A:THR252 4.5 0.0 1.0
HHB A:HEM416 4.5 0.0 1.0
HHC A:HEM416 4.6 0.0 1.0
HE22 A:GLN360 4.6 0.0 1.0
HHD A:HEM416 4.6 0.0 1.0
CB A:GLN360 4.6 0.0 1.0
N A:GLN360 4.6 0.0 1.0
N A:GLY359 4.7 0.0 1.0
H91 A:CAM415 4.7 0.0 1.0
HA3 A:GLY359 4.7 0.0 1.0
N A:LEU358 4.7 0.0 1.0
HD22 A:LEU244 4.7 0.0 1.0
H2 A:HOH3028 4.8 0.0 1.0
C A:CYS357 4.8 0.0 1.0

Reference:

E.K.Asciutto, M.Dang, S.S.Pochapsky, J.D.Madura, T.C.Pochapsky. Experimentally Restrained Molecular Dynamics Simulations For Characterizing the Open States of Cytochrome P450(Cam). Biochemistry V. 50 1664 2011.
ISSN: ISSN 0006-2960
PubMed: 21265500
DOI: 10.1021/BI101820D
Page generated: Sun Dec 13 14:48:43 2020

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