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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

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