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Iron in PDB 3pc3: Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Aminoacrylate

Enzymatic activity of Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Aminoacrylate

All present enzymatic activity of Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Aminoacrylate:
4.2.1.22;

Protein crystallography data

The structure of Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Aminoacrylate, PDB code: 3pc3 was solved by M.Koutmos, J.L.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.45 / 1.55
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 93.275, 138.815, 75.146, 90.00, 90.00, 90.00
R / Rfree (%) 14.8 / 18.8

Iron Binding Sites:

The binding sites of Iron atom in the Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Aminoacrylate (pdb code 3pc3). 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 Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Aminoacrylate, PDB code: 3pc3:

Iron binding site 1 out of 1 in 3pc3

Go back to Iron Binding Sites List in 3pc3
Iron binding site 1 out of 1 in the Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Aminoacrylate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Aminoacrylate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe701

b:10.1
occ:1.00
 FE A:HEM701 0.0 10.1 1.0
NC A:HEM701 2.0 8.9 1.0
ND A:HEM701 2.0 9.8 1.0
NB A:HEM701 2.0 9.6 1.0
NA A:HEM701 2.1 9.8 1.0
NE2 A:HIS34 2.1 9.5 1.0
SG A:CYS22 2.4 11.1 1.0
CE1 A:HIS34 3.0 10.5 1.0
C4D A:HEM701 3.0 10.2 1.0
C1D A:HEM701 3.0 9.4 1.0
C1C A:HEM701 3.0 9.9 1.0
C4C A:HEM701 3.1 10.1 1.0
C4B A:HEM701 3.1 8.9 1.0
C1B A:HEM701 3.1 9.8 1.0
C1A A:HEM701 3.1 12.0 1.0
CD2 A:HIS34 3.1 9.8 1.0
C4A A:HEM701 3.1 10.7 1.0
CHD A:HEM701 3.4 9.4 1.0
CHC A:HEM701 3.4 9.0 1.0
CB A:CYS22 3.4 13.4 1.0
CHA A:HEM701 3.4 11.9 1.0
CHB A:HEM701 3.4 10.8 1.0
CA A:CYS22 4.1 13.3 1.0
ND1 A:HIS34 4.1 10.9 1.0
CG A:HIS34 4.2 10.6 1.0
C3D A:HEM701 4.3 11.4 1.0
C2D A:HEM701 4.3 10.7 1.0
C2C A:HEM701 4.3 9.6 1.0
C3C A:HEM701 4.3 9.5 1.0
C3A A:HEM701 4.3 12.2 1.0
C2A A:HEM701 4.3 13.6 1.0
C2B A:HEM701 4.3 10.2 1.0
C3B A:HEM701 4.3 9.8 1.0
NH1 A:ARG235 4.6 10.7 1.0
N A:LYS23 4.7 11.2 1.0
C A:CYS22 4.8 12.6 1.0
CB A:TRP24 4.9 9.6 1.0
N A:TRP24 5.0 10.2 1.0
CG A:PRO33 5.0 11.6 1.0

Reference:

M.Koutmos, O.Kabil, J.L.Smith, R.Banerjee. Structural Basis For Substrate Activation and Regulation By Cystathionine Beta-Synthase (Cbs) Domains in Cystathionine {Beta}-Synthase. Proc.Natl.Acad.Sci.Usa V. 107 20958 2010.
ISSN: ISSN 0027-8424
PubMed: 21081698
DOI: 10.1073/PNAS.1011448107
Page generated: Sun Dec 13 15:17:07 2020

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