Atomistry » Iron » PDB 3fpv-3gcj » 3g6n
Atomistry »
  Iron »
    PDB 3fpv-3gcj »
      3g6n »

Iron in PDB 3g6n: Crystal Structure of An Efpdf Complex with Met-Ala-Ser

Enzymatic activity of Crystal Structure of An Efpdf Complex with Met-Ala-Ser

All present enzymatic activity of Crystal Structure of An Efpdf Complex with Met-Ala-Ser:
3.5.1.88;

Protein crystallography data

The structure of Crystal Structure of An Efpdf Complex with Met-Ala-Ser, PDB code: 3g6n was solved by K.Y.Hwang, K.H.Nam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.50
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 148.688, 148.688, 141.902, 90.00, 90.00, 120.00
R / Rfree (%) 22.5 / 24.7

Other elements in 3g6n:

The structure of Crystal Structure of An Efpdf Complex with Met-Ala-Ser also contains other interesting chemical elements:

Sodium (Na) 5 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of An Efpdf Complex with Met-Ala-Ser (pdb code 3g6n). 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 An Efpdf Complex with Met-Ala-Ser, PDB code: 3g6n:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 3g6n

Go back to Iron Binding Sites List in 3g6n
Iron binding site 1 out of 2 in the Crystal Structure of An Efpdf Complex with Met-Ala-Ser


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 An Efpdf Complex with Met-Ala-Ser within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe188

b:47.5
occ:1.00
NE2 A:HIS157 2.2 14.8 1.0
SG A:CYS114 2.3 16.8 1.0
NE2 A:HIS161 2.3 19.0 1.0
O A:HOH231 2.6 18.8 1.0
CE1 A:HIS157 3.0 14.2 1.0
CB A:CYS114 3.1 21.5 1.0
CE1 A:HIS161 3.2 18.6 1.0
O A:HOH199 3.2 25.6 1.0
CD2 A:HIS157 3.3 16.7 1.0
CD2 A:HIS161 3.4 19.8 1.0
CA A:CYS114 3.5 29.6 1.0
NE2 A:GLN65 3.5 18.8 1.0
CD A:GLN65 4.1 18.6 1.0
ND1 A:HIS157 4.2 18.1 1.0
O A:GLY113 4.2 33.2 1.0
OE1 A:GLN65 4.2 17.3 1.0
CG A:HIS157 4.3 17.8 1.0
ND1 A:HIS161 4.4 18.7 1.0
C A:CYS114 4.4 30.3 1.0
N F:MET1 4.4 62.0 1.0
CG A:HIS161 4.5 19.3 1.0
CG F:MET1 4.6 74.7 1.0
N A:LEU115 4.6 27.4 1.0
O A:HOH202 4.6 16.1 1.0
CA F:MET1 4.7 62.9 1.0
N A:CYS114 4.7 29.7 1.0
OE2 A:GLU158 4.7 27.0 1.0
C A:GLY113 4.9 32.6 1.0

Iron binding site 2 out of 2 in 3g6n

Go back to Iron Binding Sites List in 3g6n
Iron binding site 2 out of 2 in the Crystal Structure of An Efpdf Complex with Met-Ala-Ser


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 An Efpdf Complex with Met-Ala-Ser within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe188

b:59.4
occ:1.00
NE2 B:HIS161 2.3 28.0 1.0
NE2 B:HIS157 2.3 12.9 1.0
SG B:CYS114 2.6 21.2 1.0
O B:HOH247 2.6 28.7 1.0
CD2 B:HIS157 3.0 14.2 1.0
CD2 B:HIS161 3.2 25.8 1.0
CE1 B:HIS161 3.4 26.5 1.0
NE2 B:GLN65 3.4 21.6 1.0
CB B:CYS114 3.5 21.6 1.0
CE1 B:HIS157 3.5 11.5 1.0
O B:HOH194 3.7 15.4 1.0
CA B:CYS114 3.7 25.9 1.0
OE2 B:GLU158 3.9 28.5 1.0
CD B:GLN65 4.0 23.7 1.0
OE1 B:GLN65 4.1 24.5 1.0
O B:GLY113 4.2 36.0 1.0
CG B:HIS157 4.3 14.9 1.0
CG B:HIS161 4.4 26.8 1.0
ND1 B:HIS161 4.4 27.1 1.0
ND1 B:HIS157 4.5 14.4 1.0
OE1 B:GLU158 4.5 27.5 1.0
N G:MET1 4.6 75.6 1.0
CD B:GLU158 4.6 25.0 1.0
C B:CYS114 4.6 27.1 1.0
CG G:MET1 4.7 58.6 1.0
N B:LEU115 4.7 32.5 1.0
N B:CYS114 4.8 26.5 1.0
O B:HOH200 4.9 16.4 1.0
CA G:MET1 4.9 77.4 1.0
C B:GLY113 4.9 35.3 1.0

Reference:

K.H.Nam, K.H.Kim, E.E.Kim, K.Y.Hwang. Crystal Structure of An Efpdf Complex with Met-Ala-Ser Based on Crystallographic Packing. Biochem.Biophys.Res.Commun. V. 381 630 2009.
ISSN: ISSN 0006-291X
PubMed: 19249287
DOI: 10.1016/J.BBRC.2009.02.113
Page generated: Sun Aug 4 10:25:34 2024

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