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Iron in PDB 2qbm: Crystal Structure of the P450CAM G248T Mutant in the Cyanide Bound State

Enzymatic activity of Crystal Structure of the P450CAM G248T Mutant in the Cyanide Bound State

All present enzymatic activity of Crystal Structure of the P450CAM G248T Mutant in the Cyanide Bound State:
1.14.15.1;

Protein crystallography data

The structure of Crystal Structure of the P450CAM G248T Mutant in the Cyanide Bound State, PDB code: 2qbm was solved by K.Von Koenig, T.M.Makris, S.D.Sligar, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.94 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.800, 64.600, 105.500, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 22

Other elements in 2qbm:

The structure of Crystal Structure of the P450CAM G248T Mutant in the Cyanide Bound State also contains other interesting chemical elements:

Potassium (K) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the P450CAM G248T Mutant in the Cyanide Bound State (pdb code 2qbm). 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 the P450CAM G248T Mutant in the Cyanide Bound State, PDB code: 2qbm:

Iron binding site 1 out of 1 in 2qbm

Go back to Iron Binding Sites List in 2qbm
Iron binding site 1 out of 1 in the Crystal Structure of the P450CAM G248T Mutant in the Cyanide Bound State


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 the P450CAM G248T Mutant in the Cyanide Bound State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe516

b:15.6
occ:1.00
 FE A:HEM516 0.0 15.6 1.0
C A:CYN421 1.9 19.8 0.7
NA A:HEM516 2.0 14.1 1.0
NC A:HEM516 2.1 17.0 1.0
NB A:HEM516 2.1 13.7 1.0
ND A:HEM516 2.1 17.1 1.0
SG A:CYS357 2.4 15.7 1.0
N A:CYN421 2.9 22.6 0.7
C4A A:HEM516 3.0 13.5 1.0
C1C A:HEM516 3.1 14.8 1.0
C1B A:HEM516 3.1 11.8 1.0
C4C A:HEM516 3.1 18.3 1.0
C4B A:HEM516 3.1 15.6 1.0
C1D A:HEM516 3.1 16.2 1.0
C1A A:HEM516 3.1 13.6 1.0
C4D A:HEM516 3.1 13.3 1.0
CB A:CYS357 3.4 16.6 1.0
CHB A:HEM516 3.4 11.2 1.0
CHC A:HEM516 3.4 14.9 1.0
CHD A:HEM516 3.4 16.0 1.0
CHA A:HEM516 3.5 11.6 1.0
CA A:CYS357 4.2 16.3 1.0
C3A A:HEM516 4.3 13.2 1.0
C2B A:HEM516 4.3 14.4 1.0
C2C A:HEM516 4.3 17.7 1.0
C2A A:HEM516 4.3 15.4 1.0
C3C A:HEM516 4.3 18.9 1.0
C3B A:HEM516 4.3 12.2 1.0
C2D A:HEM516 4.3 15.1 1.0
C3D A:HEM516 4.4 13.5 1.0
C5 A:CAM517 4.4 24.2 1.0
N A:GLY359 4.6 15.6 1.0
C A:CYS357 4.9 16.3 1.0
N A:LEU358 4.9 16.2 1.0
CA A:GLY359 4.9 16.3 1.0
OG1 A:THR252 4.9 24.4 1.0

Reference:

T.M.Makris, K.V.Koenig, I.Schlichting, S.G.Sligar. Alteration of P450 Distal Pocket Solvent Leads to Impaired Proton Delivery and Changes in Heme Geometry. Biochemistry V. 46 14129 2007.
ISSN: ISSN 0006-2960
PubMed: 18001135
DOI: 10.1021/BI7013695
Page generated: Thu Jul 17 03:37:59 2025

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