Atomistry » Iron » PDB 5li6-5m2g » 5lx4
Atomistry »
  Iron »
    PDB 5li6-5m2g »
      5lx4 »

Iron in PDB 5lx4: Cys-Gly Dipeptidase Glij Mutant D38H

Enzymatic activity of Cys-Gly Dipeptidase Glij Mutant D38H

All present enzymatic activity of Cys-Gly Dipeptidase Glij Mutant D38H:
3.4.13.19;

Protein crystallography data

The structure of Cys-Gly Dipeptidase Glij Mutant D38H, PDB code: 5lx4 was solved by E.M.Huber, M.Groll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 98.970, 98.970, 106.050, 90.00, 90.00, 120.00
R / Rfree (%) 16.3 / 19

Iron Binding Sites:

The binding sites of Iron atom in the Cys-Gly Dipeptidase Glij Mutant D38H (pdb code 5lx4). 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 Cys-Gly Dipeptidase Glij Mutant D38H, PDB code: 5lx4:

Iron binding site 1 out of 1 in 5lx4

Go back to Iron Binding Sites List in 5lx4
Iron binding site 1 out of 1 in the Cys-Gly Dipeptidase Glij Mutant D38H


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cys-Gly Dipeptidase Glij Mutant D38H within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:80.2
occ:0.75
OE2 A:GLU134 2.0 54.6 1.0
O A:HOH696 2.6 45.3 1.0
NE2 A:HIS224 2.7 32.4 1.0
NE2 A:HIS203 2.8 55.1 0.8
CD A:GLU134 3.0 50.9 1.0
CD2 A:HIS203 3.4 51.6 0.8
CE1 A:HIS224 3.5 32.2 1.0
OE1 A:GLU134 3.5 51.4 1.0
NE2 A:HIS161 3.6 54.9 0.8
CD2 A:HIS224 3.6 26.0 1.0
CD2 A:HIS161 3.7 56.2 0.8
CE1 A:HIS203 3.8 54.5 0.8
CE1 A:HIS25 3.8 37.5 1.0
NE2 A:HIS23 3.8 34.7 1.0
OD1 A:ASP294 4.1 34.4 1.0
OD2 A:ASP294 4.2 35.1 1.0
CG A:GLU134 4.3 48.5 1.0
CD2 A:HIS23 4.3 33.2 1.0
NE2 A:HIS25 4.3 37.8 1.0
CG A:ASP294 4.4 32.9 1.0
CG A:HIS203 4.5 47.8 0.8
ND1 A:HIS224 4.6 30.9 1.0
CE1 A:HIS23 4.6 34.4 1.0
ND1 A:HIS203 4.7 51.7 0.8
CG A:HIS224 4.7 29.6 1.0
NH1 A:ARG235 4.9 48.5 1.0
CE1 A:HIS161 4.9 56.5 0.8
ND1 A:HIS25 4.9 36.0 1.0

Reference:

A.Marion, M.Groll, D.H.Scharf, K.Scherlach, M.Glaser, H.Sievers, M.Schuster, C.Hertweck, A.A.Brakhage, I.Antes, E.M.Huber. Gliotoxin Biosynthesis: Structure, Mechanism, and Metal Promiscuity of Carboxypeptidase Glij. Acs Chem. Biol. V. 12 1874 2017.
ISSN: ESSN 1554-8937
PubMed: 28525266
DOI: 10.1021/ACSCHEMBIO.6B00847
Page generated: Tue Aug 6 04:53:01 2024

Last articles

Cl in 3TAV
Cl in 3TBD
Cl in 3TBE
Cl in 3TAM
Cl in 3T88
Cl in 3TAC
Cl in 3T6U
Cl in 3T9G
Cl in 3T8M
Cl in 3T8O
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy