Iron in PDB 4l3v: Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase

All present enzymatic activity of Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase:
4.2.1.22;

The structure of Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase, PDB code: 4l3v was solved by J.Ereno, T.Majtan, I.Oyenarte, J.P.Kraus, L.A.Martinez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.52 / 3.63
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	227.750, 342.655, 107.253, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 23.2

The binding sites of Iron atom in the Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase (pdb code 4l3v). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase, PDB code: 4l3v:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase


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 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe602 b:34.4 occ:1.00 FE B:HEM602 0.0 34.4 1.0 NC B:HEM602 2.0 34.3 1.0 NA B:HEM602 2.0 34.6 1.0 NB B:HEM602 2.0 34.5 1.0 NE2 B:HIS65 2.1 7.5 1.0 ND B:HEM602 2.1 34.4 1.0 SG B:CYS52 2.2 30.2 1.0 CE1 B:HIS65 2.9 5.2 1.0 C4C B:HEM602 3.0 34.2 1.0 C4A B:HEM602 3.0 34.6 1.0 C1D B:HEM602 3.0 34.3 1.0 C1C B:HEM602 3.0 34.2 1.0 C1B B:HEM602 3.0 34.5 1.0 C1A B:HEM602 3.1 34.6 1.0 C4B B:HEM602 3.1 34.4 1.0 C4D B:HEM602 3.1 34.4 1.0 CD2 B:HIS65 3.1 5.6 1.0 CHD B:HEM602 3.3 34.2 1.0 CHB B:HEM602 3.4 34.6 1.0 CHC B:HEM602 3.5 34.3 1.0 CHA B:HEM602 3.5 34.5 1.0 CB B:CYS52 3.5 30.4 1.0 ND1 B:HIS65 4.0 5.9 1.0 CA B:CYS52 4.1 30.4 1.0 CG B:HIS65 4.1 6.8 1.0 C3C B:HEM602 4.2 34.0 1.0 C3A B:HEM602 4.2 34.7 1.0 C2C B:HEM602 4.3 34.1 1.0 C2A B:HEM602 4.3 34.7 1.0 C2D B:HEM602 4.3 34.2 1.0 C2B B:HEM602 4.3 34.6 1.0 C3B B:HEM602 4.3 34.5 1.0 C3D B:HEM602 4.3 34.4 1.0 NH1 B:ARG266 4.6 19.6 1.0 N B:THR53 4.7 35.3 1.0 C B:CYS52 4.9 29.5 1.0 CG B:PRO64 4.9 18.7 1.0 CB B:TRP54 4.9 15.8 1.0 N B:TRP54 5.0 16.8 1.0

Iron binding site 2 out of 3 in the Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe602 b:40.8 occ:1.00 FE A:HEM602 0.0 40.8 1.0 NC A:HEM602 2.0 40.6 1.0 NA A:HEM602 2.0 40.9 1.0 NE2 A:HIS65 2.1 21.1 1.0 ND A:HEM602 2.1 40.8 1.0 NB A:HEM602 2.1 40.9 1.0 SG A:CYS52 2.3 31.1 1.0 CE1 A:HIS65 2.9 21.5 1.0 C4C A:HEM602 3.0 40.5 1.0 C4A A:HEM602 3.0 41.0 1.0 C1D A:HEM602 3.0 40.6 1.0 C1A A:HEM602 3.0 41.0 1.0 C1C A:HEM602 3.1 40.6 1.0 C1B A:HEM602 3.1 40.9 1.0 C4D A:HEM602 3.1 40.8 1.0 C4B A:HEM602 3.1 40.8 1.0 CD2 A:HIS65 3.1 21.9 1.0 CHD A:HEM602 3.4 40.6 1.0 CHB A:HEM602 3.4 41.0 1.0 CHA A:HEM602 3.4 40.9 1.0 CHC A:HEM602 3.5 40.7 1.0 CB A:CYS52 3.5 31.3 1.0 ND1 A:HIS65 4.0 22.2 1.0 CG A:HIS65 4.2 19.1 1.0 CA A:CYS52 4.2 31.3 1.0 C3C A:HEM602 4.2 40.4 1.0 C3A A:HEM602 4.2 41.0 1.0 C2A A:HEM602 4.3 41.1 1.0 C2C A:HEM602 4.3 40.5 1.0 C2D A:HEM602 4.3 40.6 1.0 C2B A:HEM602 4.3 41.0 1.0 C3B A:HEM602 4.3 40.9 1.0 C3D A:HEM602 4.3 40.7 1.0 NH1 A:ARG266 4.7 13.4 1.0 CB A:TRP54 4.8 25.2 1.0 N A:THR53 4.8 32.0 1.0 CG A:PRO64 4.8 15.5 1.0 C A:CYS52 4.9 30.4 1.0 N A:TRP54 4.9 26.2 1.0

Iron binding site 3 out of 3 in the Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of DELTA516-525 Human Cystathionine Beta-Synthase within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe602 b:64.8 occ:1.00 FE C:HEM602 0.0 64.8 1.0 NB C:HEM602 2.0 64.9 1.0 NC C:HEM602 2.0 64.7 1.0 NE2 C:HIS65 2.1 28.8 1.0 ND C:HEM602 2.1 64.8 1.0 NA C:HEM602 2.1 65.0 1.0 SG C:CYS52 2.3 69.0 1.0 CE1 C:HIS65 2.9 29.1 1.0 C1B C:HEM602 3.0 65.0 1.0 C4C C:HEM602 3.0 64.6 1.0 C4B C:HEM602 3.1 64.9 1.0 C1C C:HEM602 3.1 64.7 1.0 C1D C:HEM602 3.1 64.7 1.0 C4A C:HEM602 3.1 65.0 1.0 C1A C:HEM602 3.1 65.0 1.0 C4D C:HEM602 3.1 64.9 1.0 CD2 C:HIS65 3.2 29.5 1.0 CHD C:HEM602 3.4 64.7 1.0 CHB C:HEM602 3.4 65.0 1.0 CHC C:HEM602 3.4 64.8 1.0 CHA C:HEM602 3.5 65.0 1.0 CB C:CYS52 3.5 69.2 1.0 ND1 C:HIS65 4.1 29.8 1.0 CA C:CYS52 4.2 69.3 1.0 CG C:HIS65 4.2 30.8 1.0 C2B C:HEM602 4.3 65.1 1.0 C3B C:HEM602 4.3 65.0 1.0 C3C C:HEM602 4.3 64.5 1.0 C2C C:HEM602 4.3 64.6 1.0 C2D C:HEM602 4.3 64.7 1.0 C3A C:HEM602 4.3 65.1 1.0 C2A C:HEM602 4.3 65.2 1.0 C3D C:HEM602 4.4 64.8 1.0 NH1 C:ARG266 4.7 48.7 1.0 N C:THR53 4.8 65.0 1.0 C C:CYS52 4.9 68.3 1.0 CB C:TRP54 4.9 71.2 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