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Iron in PDB 1cce: Construction of A Bis-Aquo Heme Enzyme and Replacement with Exogenous Ligand

Enzymatic activity of Construction of A Bis-Aquo Heme Enzyme and Replacement with Exogenous Ligand

All present enzymatic activity of Construction of A Bis-Aquo Heme Enzyme and Replacement with Exogenous Ligand:
1.11.1.5;

Protein crystallography data

The structure of Construction of A Bis-Aquo Heme Enzyme and Replacement with Exogenous Ligand, PDB code: 1cce was solved by D.E.Mcree, G.M.Jensen, M.M.Fitzgerald, H.A.Siegel, D.B.Goodin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 105.200, 74.300, 45.400, 90.00, 90.00, 90.00
R / Rfree (%) 19 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Construction of A Bis-Aquo Heme Enzyme and Replacement with Exogenous Ligand (pdb code 1cce). 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 Construction of A Bis-Aquo Heme Enzyme and Replacement with Exogenous Ligand, PDB code: 1cce:

Iron binding site 1 out of 1 in 1cce

Go back to Iron Binding Sites List in 1cce
Iron binding site 1 out of 1 in the Construction of A Bis-Aquo Heme Enzyme and Replacement with Exogenous Ligand


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Construction of A Bis-Aquo Heme Enzyme and Replacement with Exogenous Ligand within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1

b:18.5
occ:1.00
FE A:HEM1 0.0 18.5 1.0
O A:HOH387 2.0 24.1 1.0
O A:HOH313 2.0 11.8 1.0
NC A:HEM1 2.0 14.6 1.0
NA A:HEM1 2.1 15.3 1.0
NB A:HEM1 2.1 14.5 1.0
ND A:HEM1 2.1 18.8 1.0
C4C A:HEM1 3.0 18.5 1.0
C1A A:HEM1 3.0 19.6 1.0
C1C A:HEM1 3.0 18.0 1.0
C4D A:HEM1 3.0 17.7 1.0
C4B A:HEM1 3.1 15.6 1.0
C1D A:HEM1 3.1 13.4 1.0
C4A A:HEM1 3.1 16.9 1.0
C1B A:HEM1 3.1 14.8 1.0
CHD A:HEM1 3.3 18.1 1.0
CHA A:HEM1 3.3 19.5 1.0
CHC A:HEM1 3.4 12.6 1.0
CHB A:HEM1 3.4 15.9 1.0
HE1 A:TRP51 3.5 0.0 1.0
O A:HOH388 4.0 38.5 1.0
NE1 A:TRP51 4.2 19.9 1.0
C3C A:HEM1 4.2 12.7 1.0
C2A A:HEM1 4.2 17.8 1.0
C2C A:HEM1 4.2 14.2 1.0
C3D A:HEM1 4.2 18.1 1.0
C3A A:HEM1 4.3 12.3 1.0
C2D A:HEM1 4.3 15.5 1.0
C3B A:HEM1 4.3 18.7 1.0
C2B A:HEM1 4.3 19.8 1.0
O A:HOH300 4.4 55.2 1.0
CD A:ARG48 4.6 13.8 1.0
CD1 A:TRP51 4.6 18.1 1.0
CG A:ARG48 4.9 12.8 1.0
HH11 A:ARG48 4.9 0.0 1.0

Reference:

D.E.Mcree, G.M.Jensen, M.M.Fitzgerald, H.A.Siegel, D.B.Goodin. Construction of A Bisaquo Heme Enzyme and Binding By Exogenous Ligands. Proc.Natl.Acad.Sci.Usa V. 91 12847 1994.
ISSN: ISSN 0027-8424
PubMed: 7809133
DOI: 10.1073/PNAS.91.26.12847
Page generated: Sat Aug 3 03:14:23 2024

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