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Iron in PDB 3l63: Crystal Structure of Camphor-Bound P450CAM at Low [K+]

Enzymatic activity of Crystal Structure of Camphor-Bound P450CAM at Low [K+]

All present enzymatic activity of Crystal Structure of Camphor-Bound P450CAM at Low [K+]:
1.14.15.1;

Protein crystallography data

The structure of Crystal Structure of Camphor-Bound P450CAM at Low [K+], PDB code: 3l63 was solved by Y.-T.Lee, R.F.Wilson, I.Rupniewski, D.B.Goodin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 35.362, 98.194, 54.197, 90.00, 103.86, 90.00
R / Rfree (%) 16.4 / 19.7

Other elements in 3l63:

The structure of Crystal Structure of Camphor-Bound P450CAM at Low [K+] also contains other interesting chemical elements:

Potassium (K) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Camphor-Bound P450CAM at Low [K+] (pdb code 3l63). 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 Camphor-Bound P450CAM at Low [K+], PDB code: 3l63:

Iron binding site 1 out of 1 in 3l63

Go back to Iron Binding Sites List in 3l63
Iron binding site 1 out of 1 in the Crystal Structure of Camphor-Bound P450CAM at Low [K+]


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 Camphor-Bound P450CAM at Low [K+] within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe420

b:10.1
occ:1.00
FE A:HEM420 0.0 10.1 1.0
NB A:HEM420 2.0 9.4 1.0
NA A:HEM420 2.1 9.1 1.0
NC A:HEM420 2.1 9.6 1.0
ND A:HEM420 2.1 10.5 1.0
SG A:CYS357 2.4 10.9 1.0
C4B A:HEM420 3.0 10.1 1.0
C1C A:HEM420 3.1 10.5 1.0
C1B A:HEM420 3.1 10.8 1.0
C4A A:HEM420 3.1 9.8 1.0
C1A A:HEM420 3.1 8.5 1.0
C4D A:HEM420 3.1 9.7 1.0
C1D A:HEM420 3.1 10.7 1.0
C4C A:HEM420 3.1 9.1 1.0
CB A:CYS357 3.4 9.7 1.0
CHC A:HEM420 3.4 11.1 1.0
CHB A:HEM420 3.5 8.8 1.0
CHA A:HEM420 3.5 9.8 1.0
CHD A:HEM420 3.5 10.1 1.0
CA A:CYS357 4.0 9.9 1.0
C5 A:CAM440 4.2 11.9 1.0
C3B A:HEM420 4.3 10.9 1.0
C2B A:HEM420 4.3 11.1 1.0
C3A A:HEM420 4.3 8.5 1.0
C2C A:HEM420 4.3 11.6 1.0
C2A A:HEM420 4.3 9.3 1.0
C3D A:HEM420 4.3 10.9 1.0
C2D A:HEM420 4.3 11.8 1.0
C3C A:HEM420 4.4 10.7 1.0
N A:GLY359 4.4 10.6 1.0
N A:LEU358 4.7 10.2 1.0
C4 A:CAM440 4.7 11.8 1.0
C A:CYS357 4.7 10.6 1.0
CA A:GLY359 4.7 10.6 1.0
C9 A:CAM440 4.7 11.2 1.0

Reference:

Y.T.Lee, R.F.Wilson, I.Rupniewski, D.B.Goodin. P450CAM Visits An Open Conformation in the Absence of Substrate. Biochemistry V. 49 3412 2010.
ISSN: ISSN 0006-2960
PubMed: 20297780
DOI: 10.1021/BI100183G
Page generated: Sun Aug 4 14:06:44 2024

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