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Iron in PDB 4l4c: Structure of L358P/K178G Mutant of P450CAM Bound to Camphor

Enzymatic activity of Structure of L358P/K178G Mutant of P450CAM Bound to Camphor

All present enzymatic activity of Structure of L358P/K178G Mutant of P450CAM Bound to Camphor:
1.14.15.1;

Protein crystallography data

The structure of Structure of L358P/K178G Mutant of P450CAM Bound to Camphor, PDB code: 4l4c was solved by D.Batabyal, H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.26 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 67.581, 61.519, 94.964, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 24.3

Other elements in 4l4c:

The structure of Structure of L358P/K178G Mutant of P450CAM Bound to Camphor also contains other interesting chemical elements:

Potassium (K) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of L358P/K178G Mutant of P450CAM Bound to Camphor (pdb code 4l4c). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of L358P/K178G Mutant of P450CAM Bound to Camphor, PDB code: 4l4c:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 4l4c

Go back to Iron Binding Sites List in 4l4c
Iron binding site 1 out of 2 in the Structure of L358P/K178G Mutant of P450CAM Bound to Camphor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of L358P/K178G Mutant of P450CAM Bound to Camphor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:15.5
occ:1.00
FE A:HEM501 0.0 15.5 1.0
NB A:HEM501 2.1 10.1 1.0
NC A:HEM501 2.1 8.3 1.0
NA A:HEM501 2.1 11.0 1.0
ND A:HEM501 2.1 13.3 1.0
SG A:CYS357 2.6 14.3 1.0
C4B A:HEM501 3.1 8.5 1.0
C4C A:HEM501 3.1 10.2 1.0
C1C A:HEM501 3.1 6.8 1.0
C1B A:HEM501 3.1 14.5 1.0
C1D A:HEM501 3.1 15.7 1.0
C4D A:HEM501 3.1 8.2 1.0
C1A A:HEM501 3.1 8.8 1.0
C4A A:HEM501 3.1 11.8 1.0
CB A:CYS357 3.3 10.1 1.0
CHC A:HEM501 3.4 4.6 1.0
CHD A:HEM501 3.5 14.7 1.0
CHA A:HEM501 3.5 6.8 1.0
CHB A:HEM501 3.5 8.7 1.0
CA A:CYS357 4.1 13.2 1.0
C3B A:HEM501 4.3 9.4 1.0
C3C A:HEM501 4.3 14.2 1.0
C2C A:HEM501 4.3 9.9 1.0
C2B A:HEM501 4.3 12.5 1.0
C2D A:HEM501 4.3 10.2 1.0
C3D A:HEM501 4.3 12.5 1.0
C2A A:HEM501 4.4 5.3 1.0
C3A A:HEM501 4.4 6.6 1.0
C5 A:CAM502 4.4 12.7 1.0
CD A:PRO358 4.6 17.1 1.0
N A:GLY359 4.8 18.8 1.0
C A:CYS357 4.9 22.9 1.0
N A:PRO358 4.9 20.5 1.0
C9 A:CAM502 5.0 7.7 1.0
C4 A:CAM502 5.0 4.1 1.0

Iron binding site 2 out of 2 in 4l4c

Go back to Iron Binding Sites List in 4l4c
Iron binding site 2 out of 2 in the Structure of L358P/K178G Mutant of P450CAM Bound to Camphor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of L358P/K178G Mutant of P450CAM Bound to Camphor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:15.7
occ:1.00
FE B:HEM501 0.0 15.7 1.0
NC B:HEM501 2.1 15.6 1.0
NA B:HEM501 2.1 15.6 1.0
NB B:HEM501 2.1 16.8 1.0
ND B:HEM501 2.1 10.8 1.0
SG B:CYS357 2.5 19.1 1.0
C1C B:HEM501 3.1 12.8 1.0
C4C B:HEM501 3.1 15.6 1.0
C1A B:HEM501 3.1 15.5 1.0
C4B B:HEM501 3.1 17.5 1.0
C4D B:HEM501 3.1 13.0 1.0
C4A B:HEM501 3.1 21.0 1.0
C1D B:HEM501 3.1 14.1 1.0
C1B B:HEM501 3.1 17.4 1.0
CB B:CYS357 3.4 19.3 1.0
CHC B:HEM501 3.4 12.2 1.0
CHA B:HEM501 3.4 10.8 1.0
CHD B:HEM501 3.5 9.0 1.0
CHB B:HEM501 3.5 14.9 1.0
CA B:CYS357 4.2 22.1 1.0
C5 B:CAM502 4.3 15.1 1.0
C3C B:HEM501 4.3 19.6 1.0
C2C B:HEM501 4.3 16.0 1.0
C2A B:HEM501 4.3 16.5 1.0
C3B B:HEM501 4.3 18.9 1.0
C3A B:HEM501 4.3 18.1 1.0
C2B B:HEM501 4.4 12.6 1.0
C3D B:HEM501 4.4 15.2 1.0
C2D B:HEM501 4.4 15.2 1.0
CD B:PRO358 4.6 15.7 1.0
C4 B:CAM502 4.7 16.3 1.0
C9 B:CAM502 4.7 19.1 1.0
N B:GLY359 4.8 16.3 1.0
C B:CYS357 4.9 25.9 1.0
N B:PRO358 4.9 22.9 1.0

Reference:

D.Batabyal, H.Li, T.L.Poulos. Synergistic Effects of Mutations in Cytochrome P450CAM Designed to Mimic CYP101D1. Biochemistry V. 52 5396 2013.
ISSN: ISSN 0006-2960
PubMed: 23865948
DOI: 10.1021/BI400676D
Page generated: Sun Dec 13 15:40:46 2020

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