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Iron in PDB 1geb: X-Ray Crystal Structure and Catalytic Properties of THR252ILE Mutant of Cytochrome P450CAM

Enzymatic activity of X-Ray Crystal Structure and Catalytic Properties of THR252ILE Mutant of Cytochrome P450CAM

All present enzymatic activity of X-Ray Crystal Structure and Catalytic Properties of THR252ILE Mutant of Cytochrome P450CAM:
1.14.15.1;

Protein crystallography data

The structure of X-Ray Crystal Structure and Catalytic Properties of THR252ILE Mutant of Cytochrome P450CAM, PDB code: 1geb was solved by T.Hishiki, H.Shimada, S.Nagano, S.-Y.Park, Y.Ishimura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.03
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 106.430, 103.440, 35.000, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 22.8

Iron Binding Sites:

The binding sites of Iron atom in the X-Ray Crystal Structure and Catalytic Properties of THR252ILE Mutant of Cytochrome P450CAM (pdb code 1geb). 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 X-Ray Crystal Structure and Catalytic Properties of THR252ILE Mutant of Cytochrome P450CAM, PDB code: 1geb:

Iron binding site 1 out of 1 in 1geb

Go back to Iron Binding Sites List in 1geb
Iron binding site 1 out of 1 in the X-Ray Crystal Structure and Catalytic Properties of THR252ILE Mutant of Cytochrome P450CAM


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Crystal Structure and Catalytic Properties of THR252ILE Mutant of Cytochrome P450CAM within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe417

b:13.5
occ:1.00
 FE A:HEM417 0.0 13.5 1.0
NA A:HEM417 2.0 12.7 1.0
NC A:HEM417 2.0 14.8 1.0
ND A:HEM417 2.0 16.1 1.0
NB A:HEM417 2.0 15.1 1.0
SG A:CYS357 2.1 13.3 1.0
C4D A:HEM417 3.0 12.0 1.0
C1C A:HEM417 3.0 13.3 1.0
C1A A:HEM417 3.0 13.8 1.0
C4B A:HEM417 3.0 14.9 1.0
C4A A:HEM417 3.1 14.7 1.0
C1D A:HEM417 3.1 15.8 1.0
C1B A:HEM417 3.1 13.2 1.0
C4C A:HEM417 3.1 13.6 1.0
CB A:CYS357 3.2 14.4 1.0
CHA A:HEM417 3.4 12.7 1.0
CHC A:HEM417 3.4 12.8 1.0
CHB A:HEM417 3.5 15.1 1.0
CHD A:HEM417 3.5 14.3 1.0
CA A:CYS357 4.0 18.3 1.0
C2C A:HEM417 4.3 12.9 1.0
C3D A:HEM417 4.3 17.6 1.0
C2A A:HEM417 4.3 11.2 1.0
C3A A:HEM417 4.3 11.5 1.0
C2D A:HEM417 4.3 17.4 1.0
C3B A:HEM417 4.3 14.4 1.0
C2B A:HEM417 4.3 14.6 1.0
C3C A:HEM417 4.3 10.4 1.0
C5 A:CAM418 4.3 22.7 1.0
CD1 A:ILE252 4.4 13.6 1.0
N A:GLY359 4.7 20.9 1.0
N A:LEU358 4.7 19.2 1.0
C A:CYS357 4.7 20.2 1.0

Reference:

T.Hishiki, H.Shimada, S.Nagano, T.Egawa, Y.Kanamori, R.Makino, S.Y.Park, S.Adachi, Y.Shiro, Y.Ishimura. X-Ray Crystal Structure and Catalytic Properties of THR252ILE Mutant of Cytochrome P450CAM: Roles of THR252 and Water in the Active Center. J.Biochem. V. 128 965 2000.
ISSN: ISSN 0021-924X
PubMed: 11098139
DOI: 10.1093/OXFORDJOURNALS.JBCHEM.A022848
Page generated: Sun Dec 13 14:15:18 2020

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