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Iron in PDB 1f26: Crystal Structure of No Complex of THR243VAL Mutants of Cytochrome P450NOR

Enzymatic activity of Crystal Structure of No Complex of THR243VAL Mutants of Cytochrome P450NOR

All present enzymatic activity of Crystal Structure of No Complex of THR243VAL Mutants of Cytochrome P450NOR:
1.7.99.7;

Protein crystallography data

The structure of Crystal Structure of No Complex of THR243VAL Mutants of Cytochrome P450NOR, PDB code: 1f26 was solved by H.Shimizu, S.-Y.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.567, 81.938, 85.528, 90.00, 90.00, 90.00
R / Rfree (%) 13.9 / 20.7

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of No Complex of THR243VAL Mutants of Cytochrome P450NOR (pdb code 1f26). 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 No Complex of THR243VAL Mutants of Cytochrome P450NOR, PDB code: 1f26:

Iron binding site 1 out of 1 in 1f26

Go back to Iron Binding Sites List in 1f26
Iron binding site 1 out of 1 in the Crystal Structure of No Complex of THR243VAL Mutants of Cytochrome P450NOR


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 No Complex of THR243VAL Mutants of Cytochrome P450NOR within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:9.6
occ:1.00
FE A:HEM501 0.0 9.6 1.0
NC A:HEM501 1.9 9.6 1.0
NA A:HEM501 2.0 8.9 1.0
ND A:HEM501 2.0 9.2 1.0
N A:NO502 2.0 13.9 1.0
NB A:HEM501 2.0 9.7 1.0
SG A:CYS352 2.3 9.3 1.0
O A:NO502 2.9 19.2 1.0
C4B A:HEM501 3.0 7.9 1.0
C4A A:HEM501 3.0 9.2 1.0
C4C A:HEM501 3.0 9.3 1.0
C1C A:HEM501 3.0 9.6 1.0
C1D A:HEM501 3.1 9.4 1.0
C4D A:HEM501 3.1 9.2 1.0
C1A A:HEM501 3.1 9.1 1.0
C1B A:HEM501 3.1 8.9 1.0
CHD A:HEM501 3.4 11.4 1.0
CHB A:HEM501 3.4 9.1 1.0
CB A:CYS352 3.4 9.2 1.0
CHA A:HEM501 3.4 8.7 1.0
CHC A:HEM501 3.5 9.8 1.0
C3B A:HEM501 4.2 8.2 1.0
C2A A:HEM501 4.2 8.2 1.0
CA A:CYS352 4.3 8.4 1.0
C2C A:HEM501 4.3 8.8 1.0
C3A A:HEM501 4.3 8.9 1.0
C3C A:HEM501 4.3 9.1 1.0
C2D A:HEM501 4.3 9.1 1.0
C3D A:HEM501 4.4 8.8 1.0
C2B A:HEM501 4.4 9.2 1.0
CA A:GLY240 4.6 11.6 1.0
O A:HOH674 4.7 22.9 1.0
O A:ALA239 4.9 13.4 1.0
C A:CYS352 5.0 8.9 1.0

Reference:

E.Obayashi, H.Shimizu, S.Y.Park, H.Shoun, Y.Shiro. Mutation Effects of A Conserved Threonine (THR243) of Cytochrome P450NOR on Its Structure and Function. J.Inorg.Biochem. V. 82 103 2000.
ISSN: ISSN 0162-0134
PubMed: 11132616
DOI: 10.1016/S0162-0134(00)00161-6
Page generated: Wed Jul 16 13:55:19 2025

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