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Iron in PDB 4cpp: Crystal Structures of Cytochrome P450-Cam Complexed with Camphane, Thiocamphor, and Adamantane: Factors Controlling P450 Substrate Hydroxylation

Enzymatic activity of Crystal Structures of Cytochrome P450-Cam Complexed with Camphane, Thiocamphor, and Adamantane: Factors Controlling P450 Substrate Hydroxylation

All present enzymatic activity of Crystal Structures of Cytochrome P450-Cam Complexed with Camphane, Thiocamphor, and Adamantane: Factors Controlling P450 Substrate Hydroxylation:
1.14.15.1;

Protein crystallography data

The structure of Crystal Structures of Cytochrome P450-Cam Complexed with Camphane, Thiocamphor, and Adamantane: Factors Controlling P450 Substrate Hydroxylation, PDB code: 4cpp was solved by R.Raag, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.11
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 108.670, 103.900, 36.380, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structures of Cytochrome P450-Cam Complexed with Camphane, Thiocamphor, and Adamantane: Factors Controlling P450 Substrate Hydroxylation (pdb code 4cpp). 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 Structures of Cytochrome P450-Cam Complexed with Camphane, Thiocamphor, and Adamantane: Factors Controlling P450 Substrate Hydroxylation, PDB code: 4cpp:

Iron binding site 1 out of 1 in 4cpp

Go back to Iron Binding Sites List in 4cpp
Iron binding site 1 out of 1 in the Crystal Structures of Cytochrome P450-Cam Complexed with Camphane, Thiocamphor, and Adamantane: Factors Controlling P450 Substrate Hydroxylation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structures of Cytochrome P450-Cam Complexed with Camphane, Thiocamphor, and Adamantane: Factors Controlling P450 Substrate Hydroxylation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe417

b:12.4
occ:1.00
 FE A:HEM417 0.0 12.4 1.0
O A:HOH501 1.9 14.3 1.0
ND A:HEM417 2.0 14.3 1.0
NB A:HEM417 2.0 13.0 1.0
NA A:HEM417 2.1 13.4 1.0
NC A:HEM417 2.1 14.0 1.0
SG A:CYS357 2.1 10.8 1.0
C1D A:HEM417 3.0 15.0 1.0
C4D A:HEM417 3.1 14.2 1.0
C4B A:HEM417 3.1 13.8 1.0
C1A A:HEM417 3.1 14.0 1.0
C1C A:HEM417 3.1 13.1 1.0
C4C A:HEM417 3.1 13.8 1.0
C4A A:HEM417 3.1 13.3 1.0
C1B A:HEM417 3.1 13.3 1.0
CB A:CYS357 3.2 14.2 1.0
CHC A:HEM417 3.4 14.1 1.0
CHD A:HEM417 3.4 14.1 1.0
CHA A:HEM417 3.5 15.0 1.0
CHB A:HEM417 3.5 13.0 1.0
CA A:CYS357 4.0 14.5 1.0
C5 A:ADM422 4.2 25.3 1.0
C2D A:HEM417 4.3 14.3 1.0
C3D A:HEM417 4.3 15.0 1.0
C3B A:HEM417 4.3 13.1 1.0
C2B A:HEM417 4.3 12.9 1.0
C3C A:HEM417 4.3 14.8 1.0
C2C A:HEM417 4.3 14.0 1.0
C2A A:HEM417 4.3 14.2 1.0
C3A A:HEM417 4.3 14.1 1.0
N A:GLY359 4.7 13.6 1.0
C A:CYS357 4.7 14.6 1.0
C4 A:ADM422 4.8 23.8 1.0
C6 A:ADM422 4.8 24.1 1.0
N A:LEU358 4.9 15.5 1.0

Reference:

R.Raag, T.L.Poulos. Crystal Structures of Cytochrome P-450CAM Complexed with Camphane, Thiocamphor, and Adamantane: Factors Controlling P-450 Substrate Hydroxylation. Biochemistry V. 30 2674 1991.
ISSN: ISSN 0006-2960
PubMed: 2001355
DOI: 10.1021/BI00224A016
Page generated: Tue Aug 5 09:32:07 2025

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