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Iron in PDB 3pc4: Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Serine

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

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

Protein crystallography data

The structure of Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Serine, PDB code: 3pc4 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) 41.21 / 1.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 92.947, 137.935, 75.129, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 20.3

Other elements in 3pc4:

The structure of Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Serine also contains other interesting chemical elements:

Sodium (Na) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Serine (pdb code 3pc4). 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 Serine, PDB code: 3pc4:

Iron binding site 1 out of 1 in 3pc4

Go back to Iron Binding Sites List in 3pc4
Iron binding site 1 out of 1 in the Full Length Structure of Cystathionine Beta-Synthase From Drosophila in Complex with Serine


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 Serine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe701

b:16.4
occ:1.00
 FE A:HEM701 0.0 16.4 1.0
NB A:HEM701 2.0 15.2 1.0
ND A:HEM701 2.0 17.7 1.0
NA A:HEM701 2.1 16.1 1.0
NC A:HEM701 2.1 12.9 1.0
NE2 A:HIS34 2.1 17.0 1.0
SG A:CYS22 2.4 16.0 1.0
CE1 A:HIS34 3.0 17.2 1.0
C4B A:HEM701 3.0 15.3 1.0
C4D A:HEM701 3.0 18.5 1.0
C1B A:HEM701 3.0 16.7 1.0
C1D A:HEM701 3.1 16.6 1.0
C1A A:HEM701 3.1 19.9 1.0
C1C A:HEM701 3.1 14.6 1.0
C4C A:HEM701 3.1 14.9 1.0
C4A A:HEM701 3.1 17.7 1.0
CD2 A:HIS34 3.1 15.5 1.0
CHA A:HEM701 3.4 19.6 1.0
CHC A:HEM701 3.4 14.3 1.0
CHD A:HEM701 3.4 15.1 1.0
CHB A:HEM701 3.4 17.6 1.0
CB A:CYS22 3.5 18.9 1.0
CA A:CYS22 4.1 19.1 1.0
ND1 A:HIS34 4.2 18.2 1.0
CG A:HIS34 4.2 17.5 1.0
C3D A:HEM701 4.3 20.1 1.0
C3B A:HEM701 4.3 16.4 1.0
C2B A:HEM701 4.3 15.8 1.0
C2D A:HEM701 4.3 18.9 1.0
C2C A:HEM701 4.3 13.9 1.0
C3C A:HEM701 4.3 12.9 1.0
C2A A:HEM701 4.3 21.8 1.0
C3A A:HEM701 4.3 19.9 1.0
NH1 A:ARG235 4.5 16.2 1.0
N A:LYS23 4.7 16.7 1.0
C A:CYS22 4.9 18.4 1.0
CB A:TRP24 4.9 14.8 1.0
N A:TRP24 4.9 14.9 1.0
CG A:PRO33 5.0 18.2 1.0
CD A:PRO33 5.0 18.3 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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