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Iron in PDB 6tae: Neutron Structure of Ferric Ascorbate Peroxidase

Enzymatic activity of Neutron Structure of Ferric Ascorbate Peroxidase

All present enzymatic activity of Neutron Structure of Ferric Ascorbate Peroxidase:
1.11.1.11;

Protein crystallography data

The structure of Neutron Structure of Ferric Ascorbate Peroxidase, PDB code: 6tae was solved by H.Kwon, J.Basran, J.M.Devos, T.E.Schrader, A.Ostermann, M.P.Blakeley, E.L.Raven, P.C.E.Moody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.90
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.904, 82.904, 75.868, 90.00, 90.00, 90.00
R / Rfree (%) 27.6 / 30.8

Iron Binding Sites:

The binding sites of Iron atom in the Neutron Structure of Ferric Ascorbate Peroxidase (pdb code 6tae). 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 Neutron Structure of Ferric Ascorbate Peroxidase, PDB code: 6tae:

Iron binding site 1 out of 1 in 6tae

Go back to Iron Binding Sites List in 6tae
Iron binding site 1 out of 1 in the Neutron Structure of Ferric Ascorbate Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Neutron Structure of Ferric Ascorbate Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:23.8
occ:1.00
FE A:HEM301 0.0 23.8 1.0
NC A:HEM301 2.0 21.4 1.0
NE2 A:HIS163 2.1 22.3 1.0
NB A:HEM301 2.1 22.3 1.0
NA A:HEM301 2.1 24.1 1.0
ND A:HEM301 2.1 21.4 1.0
D1 A:DOD411 2.2 26.9 1.0
O A:DOD411 2.3 36.4 1.0
C4C A:HEM301 3.0 21.2 1.0
C1C A:HEM301 3.0 23.4 1.0
C1D A:HEM301 3.0 18.5 1.0
C4B A:HEM301 3.0 26.7 1.0
CD2 A:HIS163 3.0 21.3 1.0
CE1 A:HIS163 3.0 22.6 1.0
C1A A:HEM301 3.1 25.5 1.0
C1B A:HEM301 3.1 19.8 1.0
C4A A:HEM301 3.1 24.7 1.0
C4D A:HEM301 3.1 21.6 1.0
DE1 A:HIS163 3.2 27.8 1.0
DD2 A:HIS163 3.2 25.2 1.0
D2 A:DOD411 3.3 31.0 1.0
CHD A:HEM301 3.4 17.6 1.0
CHC A:HEM301 3.4 24.3 1.0
CHA A:HEM301 3.5 20.8 1.0
CHB A:HEM301 3.5 23.8 1.0
DE1 A:TRP41 3.5 26.9 1.0
O A:DOD467 4.1 49.7 1.0
NE1 A:TRP41 4.1 32.7 1.0
ND1 A:HIS163 4.2 23.5 1.0
CG A:HIS163 4.2 20.7 1.0
C2C A:HEM301 4.2 24.4 1.0
C3C A:HEM301 4.2 21.1 1.0
DD1 A:TRP41 4.2 32.8 1.0
C2D A:HEM301 4.2 23.8 1.0
C3B A:HEM301 4.3 28.4 1.0
C3D A:HEM301 4.3 18.6 1.0
C2B A:HEM301 4.3 26.2 1.0
C3A A:HEM301 4.3 25.2 1.0
C2A A:HEM301 4.3 22.0 1.0
HHD A:HEM301 4.3 18.4 1.0
HHC A:HEM301 4.3 30.1 1.0
HHA A:HEM301 4.4 23.4 1.0
HHB A:HEM301 4.5 22.7 1.0
CD1 A:TRP41 4.5 30.4 1.0
D1 A:DOD467 4.6 33.5 1.0
DH2 A:TRP179 4.6 24.7 1.0
DG3 A:ARG38 4.7 27.8 1.0
D2 A:DOD467 4.8 31.7 1.0
O A:DOD433 4.8 44.5 1.0
DD1 A:HIS163 4.9 22.2 1.0
DZ2 A:TRP179 5.0 29.6 1.0
D1 A:DOD433 5.0 28.6 1.0

Reference:

H.Kwon, J.Basran, J.M.Devos, R.Suardiaz, M.W.Van Der Kamp, A.J.Mulholland, T.E.Schrader, A.Ostermann, M.P.Blakeley, P.C.E.Moody, E.L.Raven. Visualizing the Protons in A Metalloenzyme Electron Proton Transfer Pathway. Proc.Natl.Acad.Sci.Usa 2020.
ISSN: ESSN 1091-6490
PubMed: 32152099
DOI: 10.1073/PNAS.1918936117
Page generated: Sun Dec 13 17:08:51 2020

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