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Iron in PDB 4kky: Crystal Structure of N-(1-Pyrene)Acetamide Labeled P450CAM in Substrate Bound Form.

Enzymatic activity of Crystal Structure of N-(1-Pyrene)Acetamide Labeled P450CAM in Substrate Bound Form.

All present enzymatic activity of Crystal Structure of N-(1-Pyrene)Acetamide Labeled P450CAM in Substrate Bound Form.:
1.14.15.1;

Protein crystallography data

The structure of Crystal Structure of N-(1-Pyrene)Acetamide Labeled P450CAM in Substrate Bound Form., PDB code: 4kky was solved by M.Zhang, D.B.Goodin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.27 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 35.950, 101.990, 57.350, 90.00, 101.73, 90.00
R / Rfree (%) 17 / 22.5

Other elements in 4kky:

The structure of Crystal Structure of N-(1-Pyrene)Acetamide Labeled P450CAM in Substrate Bound Form. also contains other interesting chemical elements:

Potassium (K) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of N-(1-Pyrene)Acetamide Labeled P450CAM in Substrate Bound Form. (pdb code 4kky). 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 Crystal Structure of N-(1-Pyrene)Acetamide Labeled P450CAM in Substrate Bound Form., PDB code: 4kky:

Iron binding site 1 out of 1 in 4kky

Go back to Iron Binding Sites List in 4kky
Iron binding site 1 out of 1 in the Crystal Structure of N-(1-Pyrene)Acetamide Labeled P450CAM in Substrate Bound Form.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of N-(1-Pyrene)Acetamide Labeled P450CAM in Substrate Bound Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Fe501

b:14.4
occ:1.00
 FE X:HEM501 0.0 14.4 1.0
NA X:HEM501 2.0 13.9 1.0
NC X:HEM501 2.0 13.8 1.0
NB X:HEM501 2.1 13.6 1.0
ND X:HEM501 2.1 15.0 1.0
SG X:CYS357 2.3 13.4 1.0
C1A X:HEM501 3.0 12.8 1.0
C4A X:HEM501 3.1 13.4 1.0
C4B X:HEM501 3.1 13.8 1.0
C1B X:HEM501 3.1 14.1 1.0
C4D X:HEM501 3.1 14.6 1.0
C1C X:HEM501 3.1 13.5 1.0
C1D X:HEM501 3.1 14.3 1.0
C4C X:HEM501 3.2 14.3 1.0
CB X:CYS357 3.4 13.2 1.0
CHA X:HEM501 3.4 12.5 1.0
CHC X:HEM501 3.5 13.2 1.0
CHB X:HEM501 3.5 12.8 1.0
CHD X:HEM501 3.6 14.5 1.0
CA X:CYS357 4.0 13.1 1.0
C5 X:CAM503 4.1 13.3 1.0
C2A X:HEM501 4.3 13.9 1.0
C3A X:HEM501 4.4 13.5 1.0
C3B X:HEM501 4.4 12.8 1.0
C2B X:HEM501 4.4 13.1 1.0
C3D X:HEM501 4.4 14.7 1.0
C2D X:HEM501 4.4 15.0 1.0
C2C X:HEM501 4.4 13.6 1.0
N X:GLY359 4.5 13.7 1.0
C3C X:HEM501 4.5 14.8 1.0
N X:LEU358 4.7 12.2 1.0
C4 X:CAM503 4.7 13.7 1.0
C X:CYS357 4.7 12.7 1.0
C9 X:CAM503 4.9 13.2 1.0
CA X:GLY359 4.9 14.2 1.0

Reference:

M.Zhang, D.B.Goodin. To Be Determined. To Be Published.
Page generated: Sun Dec 13 15:39:48 2020

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