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Iron in PDB 2eus: Cytochrome C Peroxidase (Ccp) in Complex with Benzylamine

Enzymatic activity of Cytochrome C Peroxidase (Ccp) in Complex with Benzylamine

All present enzymatic activity of Cytochrome C Peroxidase (Ccp) in Complex with Benzylamine:
1.11.1.5;

Protein crystallography data

The structure of Cytochrome C Peroxidase (Ccp) in Complex with Benzylamine, PDB code: 2eus was solved by R.Brenk, S.W.Vetter, S.E.Boyce, D.B.Goodin, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.890, 73.830, 105.060, 90.00, 90.00, 90.00
R / Rfree (%) 14.8 / 17.8

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome C Peroxidase (Ccp) in Complex with Benzylamine (pdb code 2eus). 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 Cytochrome C Peroxidase (Ccp) in Complex with Benzylamine, PDB code: 2eus:

Iron binding site 1 out of 1 in 2eus

Go back to Iron Binding Sites List in 2eus
Iron binding site 1 out of 1 in the Cytochrome C Peroxidase (Ccp) in Complex with Benzylamine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Peroxidase (Ccp) in Complex with Benzylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe295

b:7.9
occ:1.00
FE A:HEM295 0.0 7.9 1.0
NC A:HEM295 2.0 12.5 1.0
NB A:HEM295 2.0 12.5 1.0
NA A:HEM295 2.0 12.5 1.0
NE2 A:HIS175 2.0 8.3 1.0
ND A:HEM295 2.0 12.5 1.0
O A:HOH716 2.2 20.2 1.0
C1C A:HEM295 3.0 6.9 1.0
CE1 A:HIS175 3.0 8.5 1.0
C4C A:HEM295 3.0 7.1 1.0
CD2 A:HIS175 3.0 8.5 1.0
C4B A:HEM295 3.0 7.8 1.0
C1D A:HEM295 3.0 7.6 1.0
C1B A:HEM295 3.1 7.5 1.0
C4A A:HEM295 3.1 6.6 1.0
C1A A:HEM295 3.1 6.8 1.0
C4D A:HEM295 3.1 6.2 1.0
CHC A:HEM295 3.4 7.3 1.0
CHB A:HEM295 3.4 6.9 1.0
CHD A:HEM295 3.4 7.1 1.0
CHA A:HEM295 3.4 6.3 1.0
NE1 A:TRP51 4.0 10.4 1.0
ND1 A:HIS175 4.1 7.7 1.0
O A:HOH665 4.1 17.0 1.0
CG A:HIS175 4.2 8.3 1.0
NE A:ARG48 4.2 10.6 1.0
C2C A:HEM295 4.2 7.1 1.0
C3C A:HEM295 4.2 7.8 1.0
C3B A:HEM295 4.3 7.7 1.0
C2B A:HEM295 4.3 6.8 1.0
C2A A:HEM295 4.3 7.3 1.0
C2D A:HEM295 4.3 8.1 1.0
C3D A:HEM295 4.3 6.9 1.0
C3A A:HEM295 4.3 9.3 1.0
CD1 A:TRP51 4.6 11.0 1.0
NH2 A:ARG48 4.7 10.9 1.0
C3 A:ABN400 4.7 8.6 1.0
CG A:ARG48 4.9 7.2 1.0
CZ A:ARG48 4.9 9.9 1.0

Reference:

R.Brenk, S.W.Vetter, S.E.Boyce, D.B.Goodin, B.K.Shoichet. Probing Molecular Docking in A Charged Model Binding Site. J.Mol.Biol. V. 357 1449 2006.
ISSN: ISSN 0022-2836
PubMed: 16490206
DOI: 10.1016/J.JMB.2006.01.034
Page generated: Sat Aug 3 21:10:00 2024

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