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Iron in PDB 7f30: Crystal Structure of Oxdb E85A in Complex with Z-2- (3-Bromophenyl) Propanal Oxime

Enzymatic activity of Crystal Structure of Oxdb E85A in Complex with Z-2- (3-Bromophenyl) Propanal Oxime

All present enzymatic activity of Crystal Structure of Oxdb E85A in Complex with Z-2- (3-Bromophenyl) Propanal Oxime:
4.99.1.7;

Protein crystallography data

The structure of Crystal Structure of Oxdb E85A in Complex with Z-2- (3-Bromophenyl) Propanal Oxime, PDB code: 7f30 was solved by N.Muraki, D.Matsui, Y.Asano, S.Aono, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.79 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.922, 64.685, 52.563, 90, 90.49, 90
R / Rfree (%) 18.4 / 21.7

Other elements in 7f30:

The structure of Crystal Structure of Oxdb E85A in Complex with Z-2- (3-Bromophenyl) Propanal Oxime also contains other interesting chemical elements:

Bromine (Br) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Oxdb E85A in Complex with Z-2- (3-Bromophenyl) Propanal Oxime (pdb code 7f30). 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 Oxdb E85A in Complex with Z-2- (3-Bromophenyl) Propanal Oxime, PDB code: 7f30:

Iron binding site 1 out of 1 in 7f30

Go back to Iron Binding Sites List in 7f30
Iron binding site 1 out of 1 in the Crystal Structure of Oxdb E85A in Complex with Z-2- (3-Bromophenyl) Propanal Oxime


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 Oxdb E85A in Complex with Z-2- (3-Bromophenyl) Propanal Oxime within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:31.9
occ:1.00
 FE A:HEM401 0.0 31.9 1.0
NA A:HEM401 2.0 31.9 1.0
ND A:HEM401 2.1 35.9 1.0
NB A:HEM401 2.1 26.9 1.0
NC A:HEM401 2.1 30.4 1.0
NE2 A:HIS282 2.4 34.4 1.0
N04 A:0WQ402 2.8 39.9 1.0
C4B A:HEM401 3.1 32.3 1.0
C1A A:HEM401 3.1 30.0 1.0
C4A A:HEM401 3.1 31.2 1.0
C4D A:HEM401 3.1 34.6 1.0
C1D A:HEM401 3.1 32.9 1.0
C1B A:HEM401 3.1 29.0 1.0
C4C A:HEM401 3.1 33.1 1.0
C1C A:HEM401 3.1 34.4 1.0
C03 A:0WQ402 3.3 37.7 1.0
CD2 A:HIS282 3.3 30.6 1.0
CE1 A:HIS282 3.3 35.0 1.0
CHD A:HEM401 3.4 29.8 1.0
CHA A:HEM401 3.4 31.4 1.0
CHB A:HEM401 3.4 27.7 1.0
CHC A:HEM401 3.4 31.9 1.0
O05 A:0WQ402 3.6 36.7 1.0
C3B A:HEM401 4.3 29.9 1.0
C3A A:HEM401 4.3 29.3 1.0
C3D A:HEM401 4.3 35.7 1.0
C2A A:HEM401 4.3 31.7 1.0
C2B A:HEM401 4.3 29.8 1.0
C2D A:HEM401 4.3 37.2 1.0
C3C A:HEM401 4.3 28.4 1.0
C2C A:HEM401 4.3 32.1 1.0
ND1 A:HIS282 4.4 37.1 1.0
CG A:HIS282 4.5 31.2 1.0
C02 A:0WQ402 4.6 43.2 1.0
CG2 A:THR276 4.7 33.0 1.0
OG1 A:THR202 4.9 33.4 1.0

Reference:

D.Matsui, N.Muraki, K.Chen, T.Mori, A.A.Ingram, K.Oike, H.Groger, S.Aono, Y.Asano. Crystal Structural Analysis of Aldoxime Dehydratase From Bacillus Sp. Oxb-1: Importance of Surface Residues in Optimization For Crystallization. J.Inorg.Biochem. V. 230 11770 2022.
ISSN: ISSN 0162-0134
PubMed: 35272237
DOI: 10.1016/J.JINORGBIO.2022.111770
Page generated: Wed Aug 6 22:23:19 2025

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