Atomistry » Iron » PDB 5mms-5o10 » 5nws
Atomistry »
  Iron »
    PDB 5mms-5o10 »
      5nws »

Iron in PDB 5nws: Crystal Structure of Saacmm Involved in Actinomycin Biosynthesis

Protein crystallography data

The structure of Crystal Structure of Saacmm Involved in Actinomycin Biosynthesis, PDB code: 5nws was solved by R.Driller, S.Semsary, I.Crnovicic, J.Vater, U.Keller, B.Loll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.04 / 2.23
Space group C 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 79.254, 129.539, 111.611, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 22

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Saacmm Involved in Actinomycin Biosynthesis (pdb code 5nws). 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 Saacmm Involved in Actinomycin Biosynthesis, PDB code: 5nws:

Iron binding site 1 out of 1 in 5nws

Go back to Iron Binding Sites List in 5nws
Iron binding site 1 out of 1 in the Crystal Structure of Saacmm Involved in Actinomycin Biosynthesis


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 Saacmm Involved in Actinomycin Biosynthesis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe504

b:25.1
occ:1.00
FE A:HEM504 0.0 25.1 1.0
NA A:HEM504 2.0 21.6 1.0
ND A:HEM504 2.0 24.8 1.0
NB A:HEM504 2.1 21.7 1.0
NC A:HEM504 2.1 23.7 1.0
O A:HOH638 2.2 31.0 1.0
SG A:CYS382 2.4 24.2 1.0
C1A A:HEM504 3.0 21.2 1.0
C4A A:HEM504 3.0 22.6 1.0
C4D A:HEM504 3.0 23.1 1.0
C1D A:HEM504 3.0 22.5 1.0
C4C A:HEM504 3.0 23.5 1.0
C4B A:HEM504 3.1 24.0 1.0
C1B A:HEM504 3.1 21.2 1.0
C1C A:HEM504 3.1 25.4 1.0
CB A:CYS382 3.3 19.8 1.0
CHA A:HEM504 3.4 22.0 1.0
CHD A:HEM504 3.4 20.5 1.0
CHB A:HEM504 3.4 22.8 1.0
CHC A:HEM504 3.5 23.0 1.0
CA A:CYS382 4.0 20.7 1.0
C3A A:HEM504 4.2 21.8 1.0
C2A A:HEM504 4.2 22.5 1.0
C2D A:HEM504 4.3 28.6 1.0
C3D A:HEM504 4.3 23.7 1.0
C3C A:HEM504 4.3 25.8 1.0
C3B A:HEM504 4.3 20.2 1.0
C2C A:HEM504 4.3 28.5 1.0
C2B A:HEM504 4.3 21.2 1.0
O A:ALA267 4.4 28.8 1.0
C A:CYS382 4.7 23.0 1.0
N A:GLY384 4.8 22.8 1.0
CB A:ALA267 4.8 22.8 1.0
N A:LEU383 4.9 23.4 1.0

Reference:

S.Semsary, I.Crnovcic, R.Driller, J.Vater, B.Loll, U.Keller. Ketonization of Proline Residues in the Peptide Chains of Actinomycins By A 4-Oxoproline Synthase. Chembiochem V. 19 706 2018.
ISSN: ESSN 1439-7633
PubMed: 29327817
DOI: 10.1002/CBIC.201700666
Page generated: Tue Aug 6 06:20:12 2024

Last articles

Cl in 3TJI
Cl in 3TL9
Cl in 3TKW
Cl in 3TKG
Cl in 3TKD
Cl in 3TK3
Cl in 3TJQ
Cl in 3TK6
Cl in 3TK5
Cl in 3TJY
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy