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Iron in PDB 1xen: High Resolution Crystal Structure of Escherichia Coli Iron- Peptide Deformylase Bound to Formate

Enzymatic activity of High Resolution Crystal Structure of Escherichia Coli Iron- Peptide Deformylase Bound to Formate

All present enzymatic activity of High Resolution Crystal Structure of Escherichia Coli Iron- Peptide Deformylase Bound to Formate:
3.5.1.88;

Protein crystallography data

The structure of High Resolution Crystal Structure of Escherichia Coli Iron- Peptide Deformylase Bound to Formate, PDB code: 1xen was solved by R.Jain, B.Hao, R.-P.Liu, M.K.Chan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.61 / 1.85
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 54.820, 54.820, 224.580, 90.00, 90.00, 120.00
R / Rfree (%) 17.3 / 21.8

Iron Binding Sites:

The binding sites of Iron atom in the High Resolution Crystal Structure of Escherichia Coli Iron- Peptide Deformylase Bound to Formate (pdb code 1xen). 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 High Resolution Crystal Structure of Escherichia Coli Iron- Peptide Deformylase Bound to Formate, PDB code: 1xen:

Iron binding site 1 out of 1 in 1xen

Go back to Iron Binding Sites List in 1xen
Iron binding site 1 out of 1 in the High Resolution Crystal Structure of Escherichia Coli Iron- Peptide Deformylase Bound to Formate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of High Resolution Crystal Structure of Escherichia Coli Iron- Peptide Deformylase Bound to Formate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:14.2
occ:1.00
 NE2 A:HIS132 2.1 11.9 1.0
NE2 A:HIS136 2.1 13.4 1.0
O2 A:FMT301 2.3 15.0 1.0
SG A:CYS90 2.4 12.1 1.0
O1 A:FMT301 2.4 20.0 1.0
C A:FMT301 2.7 19.3 1.0
CE1 A:HIS136 3.0 11.7 1.0
CE1 A:HIS132 3.1 13.7 1.0
CD2 A:HIS132 3.1 13.2 1.0
CD2 A:HIS136 3.2 12.2 1.0
CB A:CYS90 3.3 12.5 1.0
NE2 A:GLN50 3.5 13.4 1.0
O A:HOH368 3.7 12.8 1.0
CA A:CYS90 3.7 11.5 1.0
CD A:GLN50 4.0 12.3 1.0
OE1 A:GLN50 4.0 13.4 1.0
N A:LEU91 4.1 13.4 1.0
ND1 A:HIS136 4.2 13.4 1.0
ND1 A:HIS132 4.3 11.6 1.0
CG A:HIS132 4.3 10.2 1.0
CG A:HIS136 4.3 9.6 1.0
C A:CYS90 4.3 12.5 1.0
OE1 A:GLU133 4.6 13.6 1.0
O A:GLY89 4.6 13.6 1.0
O A:HOH307 4.7 10.6 1.0
O A:HOH407 4.7 30.1 1.0
OE2 A:GLU133 4.8 17.6 1.0
N A:SER92 4.9 13.5 1.0
N A:CYS90 5.0 10.8 1.0

Reference:

R.Jain, B.Hao, R.-P.Liu, M.K.Chan. Structures of E. Coli Peptide Deformylase Bound to Formate: Insight Into the Preference For FE2+ Over ZN2+ As the Active Site Metal J.Am.Chem.Soc. V. 127 4558 2005.
ISSN: ISSN 0002-7863
PubMed: 15796505
DOI: 10.1021/JA0503074
Page generated: Wed Jul 16 22:05:32 2025

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