Iron in PDB 4l0d: Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase Containing C-Terminal 6XHIS-Tag

All present enzymatic activity of Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase Containing C-Terminal 6XHIS-Tag:
4.2.1.22;

The structure of Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase Containing C-Terminal 6XHIS-Tag, PDB code: 4l0d was solved by J.Ereno, T.Majtan, I.Oyenarte, J.P.Kraus, L.A.Martinez-Cruz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	53.06 / 2.97
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	124.365, 136.203, 169.307, 90.00, 90.00, 90.00
R / Rfree (%)	24 / 28.4

The binding sites of Iron atom in the Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase Containing C-Terminal 6XHIS-Tag (pdb code 4l0d). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase Containing C-Terminal 6XHIS-Tag, PDB code: 4l0d:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase Containing C-Terminal 6XHIS-Tag


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase Containing C-Terminal 6XHIS-Tag within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe602 b:0.7 occ:1.00 FE A:HEM602 0.0 0.7 1.0 NB A:HEM602 2.0 0.6 1.0 ND A:HEM602 2.0 0.6 1.0 NE2 A:HIS65 2.1 69.7 1.0 NC A:HEM602 2.1 0.5 1.0 NA A:HEM602 2.1 0.6 1.0 SG A:CYS52 2.2 0.1 1.0 CE1 A:HIS65 3.0 66.3 1.0 C4B A:HEM602 3.1 0.7 1.0 C1C A:HEM602 3.1 0.6 1.0 C4D A:HEM602 3.1 0.8 1.0 C1B A:HEM602 3.1 0.8 1.0 CD2 A:HIS65 3.1 69.0 1.0 C1A A:HEM602 3.1 0.8 1.0 C4A A:HEM602 3.1 0.7 1.0 C4C A:HEM602 3.1 0.8 1.0 C1D A:HEM602 3.2 0.8 1.0 CHC A:HEM602 3.5 0.7 1.0 CB A:CYS52 3.5 0.9 1.0 CHA A:HEM602 3.5 0.9 1.0 CHB A:HEM602 3.5 0.8 1.0 CHD A:HEM602 3.6 0.9 1.0 ND1 A:HIS65 4.1 68.7 1.0 C2B A:HEM602 4.2 0.9 1.0 C3B A:HEM602 4.2 0.9 1.0 C3D A:HEM602 4.2 0.9 1.0 CA A:CYS52 4.2 0.6 1.0 C2D A:HEM602 4.2 0.9 1.0 CG A:HIS65 4.2 77.3 1.0 C2C A:HEM602 4.3 0.8 1.0 C3C A:HEM602 4.3 0.9 1.0 C2A A:HEM602 4.3 0.9 1.0 C3A A:HEM602 4.3 0.9 1.0 CB A:TRP54 4.7 1.0 1.0 NH1 A:ARG266 4.8 89.3 1.0 N A:THR53 4.8 0.9 1.0 C A:CYS52 4.9 0.2 1.0 N A:TRP54 4.9 0.7 1.0

Iron binding site 2 out of 2 in the Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase Containing C-Terminal 6XHIS-Tag


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase Containing C-Terminal 6XHIS-Tag within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe602 b:0.7 occ:1.00 FE B:HEM602 0.0 0.7 1.0 NB B:HEM602 2.0 0.8 1.0 ND B:HEM602 2.0 0.8 1.0 NE2 B:HIS65 2.1 80.4 1.0 NC B:HEM602 2.1 0.7 1.0 NA B:HEM602 2.1 0.8 1.0 SG B:CYS52 2.2 98.5 1.0 CE1 B:HIS65 3.0 76.0 1.0 C4B B:HEM602 3.1 1.0 1.0 CD2 B:HIS65 3.1 79.0 1.0 C4D B:HEM602 3.1 0.1 1.0 C1C B:HEM602 3.1 0.9 1.0 C1B B:HEM602 3.1 0.0 1.0 C1A B:HEM602 3.1 0.1 1.0 C4A B:HEM602 3.1 0.0 1.0 C4C B:HEM602 3.1 0.0 1.0 C1D B:HEM602 3.2 0.0 1.0 CHC B:HEM602 3.5 0.0 1.0 CHA B:HEM602 3.5 0.2 1.0 CB B:CYS52 3.5 0.2 1.0 CHB B:HEM602 3.5 0.2 1.0 CHD B:HEM602 3.6 0.2 1.0 ND1 B:HIS65 4.1 78.6 1.0 C3B B:HEM602 4.2 0.2 1.0 C3D B:HEM602 4.2 0.3 1.0 C2B B:HEM602 4.2 0.2 1.0 CG B:HIS65 4.2 88.8 1.0 C2D B:HEM602 4.2 0.3 1.0 CA B:CYS52 4.3 0.4 1.0 C2C B:HEM602 4.3 0.2 1.0 C3C B:HEM602 4.3 0.2 1.0 C2A B:HEM602 4.3 0.3 1.0 C3A B:HEM602 4.3 0.3 1.0 CB B:TRP54 4.9 76.9 1.0 NH1 B:ARG266 4.9 73.9 1.0 N B:THR53 4.9 0.8 1.0

J.Ereno-Orbea, T.Majtan, I.Oyenarte, J.P.Kraus, L.A.Martinez-Cruz. Structural Basis of Regulation and Oligomerization of Human Cystathionine Beta-Synthase, the Central Enzyme of Transsulfuration. Proc.Natl.Acad.Sci.Usa V. 110 E3790 2013.
ISSN: ISSN 0027-8424
PubMed: 24043838
DOI: 10.1073/PNAS.1313683110