Atomistry » Iron » PDB 2vm0-2w3g » 2vz7
Atomistry »
  Iron »
    PDB 2vm0-2w3g »
      2vz7 »

Iron in PDB 2vz7: Crystal Structure of the Yc-17-Bound Pikc D50N Mutant

Protein crystallography data

The structure of Crystal Structure of the Yc-17-Bound Pikc D50N Mutant, PDB code: 2vz7 was solved by S.Li, D.H.Sherman, L.M.Podust, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.67 / 3.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.862, 109.323, 153.040, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 26

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Yc-17-Bound Pikc D50N Mutant (pdb code 2vz7). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the Yc-17-Bound Pikc D50N Mutant, PDB code: 2vz7:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 2vz7

Go back to Iron Binding Sites List in 2vz7
Iron binding site 1 out of 2 in the Crystal Structure of the Yc-17-Bound Pikc D50N Mutant


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 Yc-17-Bound Pikc D50N Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1407

b:29.1
occ:1.00
FE A:HEM1407 0.0 29.1 1.0
NC A:HEM1407 2.0 28.9 1.0
NB A:HEM1407 2.0 29.8 1.0
NA A:HEM1407 2.0 30.3 1.0
ND A:HEM1407 2.0 30.6 1.0
SG A:CYS354 2.8 38.9 1.0
C1C A:HEM1407 3.0 29.2 1.0
C4B A:HEM1407 3.0 29.4 1.0
C4C A:HEM1407 3.0 28.1 1.0
C1D A:HEM1407 3.0 30.2 1.0
C1A A:HEM1407 3.0 30.4 1.0
C1B A:HEM1407 3.0 30.9 1.0
C4A A:HEM1407 3.1 30.5 1.0
C4D A:HEM1407 3.1 30.1 1.0
CHC A:HEM1407 3.4 29.9 1.0
CHD A:HEM1407 3.4 28.4 1.0
CHA A:HEM1407 3.4 30.8 1.0
CHB A:HEM1407 3.5 30.8 1.0
CB A:CYS354 3.6 35.5 1.0
O A:ALA243 4.0 45.7 1.0
CA A:CYS354 4.1 34.0 1.0
C2D A:HEM1407 4.3 31.4 1.0
C3B A:HEM1407 4.3 29.4 1.0
C3A A:HEM1407 4.3 30.0 1.0
C3C A:HEM1407 4.3 28.2 1.0
C2A A:HEM1407 4.3 29.4 1.0
C2B A:HEM1407 4.3 29.7 1.0
C2C A:HEM1407 4.3 28.7 1.0
C3D A:HEM1407 4.3 30.8 1.0
C1 A:PXI1408 4.6 47.1 1.0
N A:ILE355 4.7 29.3 1.0
N A:GLY356 4.7 29.0 1.0
C A:ALA243 4.8 44.5 1.0
C A:CYS354 4.8 31.6 1.0
CB A:ALA243 4.9 40.7 1.0

Iron binding site 2 out of 2 in 2vz7

Go back to Iron Binding Sites List in 2vz7
Iron binding site 2 out of 2 in the Crystal Structure of the Yc-17-Bound Pikc D50N Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the Yc-17-Bound Pikc D50N Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1407

b:29.5
occ:1.00
FE B:HEM1407 0.0 29.5 1.0
ND B:HEM1407 1.9 30.2 1.0
NA B:HEM1407 1.9 29.7 1.0
NC B:HEM1407 2.0 30.8 1.0
NB B:HEM1407 2.0 30.1 1.0
SG B:CYS354 2.9 32.9 1.0
C4D B:HEM1407 3.0 31.4 1.0
C1A B:HEM1407 3.0 29.9 1.0
C1D B:HEM1407 3.0 30.2 1.0
C4A B:HEM1407 3.0 30.2 1.0
C4C B:HEM1407 3.1 30.6 1.0
C1C B:HEM1407 3.1 31.4 1.0
C1B B:HEM1407 3.1 30.1 1.0
C4B B:HEM1407 3.1 30.1 1.0
CHA B:HEM1407 3.4 30.8 1.0
CHD B:HEM1407 3.4 29.5 1.0
CHB B:HEM1407 3.4 29.6 1.0
CHC B:HEM1407 3.5 31.5 1.0
CB B:CYS354 3.6 33.2 1.0
CA B:CYS354 4.2 33.4 1.0
C3D B:HEM1407 4.2 32.1 1.0
C2D B:HEM1407 4.2 31.4 1.0
C2A B:HEM1407 4.2 28.8 1.0
C3A B:HEM1407 4.2 29.8 1.0
C3C B:HEM1407 4.3 32.0 1.0
C2C B:HEM1407 4.3 31.2 1.0
C2B B:HEM1407 4.3 30.1 1.0
C3B B:HEM1407 4.3 29.7 1.0
C1 B:PXI1408 4.4 36.3 1.0
N B:ILE355 4.9 31.6 1.0
CB B:ALA243 4.9 40.7 1.0
OG1 B:THR247 5.0 44.5 1.0
C B:CYS354 5.0 33.4 1.0

Reference:

S.Li, H.Ouellet, D.H.Sherman, L.M.Podust. Analysis of Transient and Catalytic Desosamine Binding Pockets in Cytochrome P450 Pikc From Streptomyces Venezuelae. J.Biol.Chem. V. 284 5723 2009.
ISSN: ISSN 0021-9258
PubMed: 19124459
DOI: 10.1074/JBC.M807592200
Page generated: Thu Jul 17 04:48:14 2025

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy