Iron in PDB 7qgt: Crystal Structure of Human Cystathionine Beta-Synthase (DELTA516-525) in Complex with Aoaa.

All present enzymatic activity of Crystal Structure of Human Cystathionine Beta-Synthase (DELTA516-525) in Complex with Aoaa.:
4.2.1.22;

The structure of Crystal Structure of Human Cystathionine Beta-Synthase (DELTA516-525) in Complex with Aoaa., PDB code: 7qgt was solved by A.Hutchin, J.Kopec, T.Majtan, K.Zuhra, C.Szabo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.97 / 2.69
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	125.553, 134.573, 169.291, 90, 90, 90
R / Rfree (%)	20.8 / 24.2

The binding sites of Iron atom in the Crystal Structure of Human Cystathionine Beta-Synthase (DELTA516-525) in Complex with Aoaa. (pdb code 7qgt). 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 Human Cystathionine Beta-Synthase (DELTA516-525) in Complex with Aoaa., PDB code: 7qgt:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Human Cystathionine Beta-Synthase (DELTA516-525) in Complex with Aoaa.


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 Human Cystathionine Beta-Synthase (DELTA516-525) in Complex with Aoaa. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1000 b:59.5 occ:1.00 FE A:HEM1000 0.0 59.5 1.0 NE2 A:HIS65 1.9 66.0 1.0 NC A:HEM1000 2.1 59.4 1.0 ND A:HEM1000 2.1 59.5 1.0 NB A:HEM1000 2.1 59.4 1.0 NA A:HEM1000 2.1 59.6 1.0 SG A:CYS52 2.7 53.2 1.0 CD2 A:HIS65 2.9 65.1 1.0 CE1 A:HIS65 3.0 66.1 1.0 C1C A:HEM1000 3.0 59.2 1.0 C1A A:HEM1000 3.0 59.8 1.0 C1B A:HEM1000 3.1 59.3 1.0 C4C A:HEM1000 3.1 59.3 1.0 C4A A:HEM1000 3.1 59.6 1.0 C4D A:HEM1000 3.1 59.5 1.0 C4B A:HEM1000 3.1 59.2 1.0 C1D A:HEM1000 3.1 59.5 1.0 CHC A:HEM1000 3.4 59.2 1.0 CHA A:HEM1000 3.4 59.6 1.0 CHB A:HEM1000 3.4 59.5 1.0 CHD A:HEM1000 3.5 59.3 1.0 CB A:CYS52 3.7 50.8 1.0 CG A:HIS65 4.0 64.3 1.0 ND1 A:HIS65 4.1 65.7 1.0 C2C A:HEM1000 4.3 59.0 1.0 C3C A:HEM1000 4.3 59.0 1.0 C2A A:HEM1000 4.3 60.2 1.0 C3A A:HEM1000 4.3 60.0 1.0 C3B A:HEM1000 4.3 59.1 1.0 C2B A:HEM1000 4.3 59.0 1.0 C3D A:HEM1000 4.3 59.1 1.0 C2D A:HEM1000 4.3 59.3 1.0 CA A:CYS52 4.4 50.5 1.0 NH1 A:ARG266 4.7 43.6 1.0 CD A:PRO64 4.8 63.5 1.0 CG A:PRO64 5.0 64.8 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Human Cystathionine Beta-Synthase (DELTA516-525) in Complex with Aoaa.


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 Human Cystathionine Beta-Synthase (DELTA516-525) in Complex with Aoaa. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1000 b:69.3 occ:1.00 FE B:HEM1000 0.0 69.3 1.0 NE2 B:HIS65 2.0 76.8 1.0 NC B:HEM1000 2.1 69.0 1.0 NB B:HEM1000 2.1 69.4 1.0 NA B:HEM1000 2.1 69.5 1.0 ND B:HEM1000 2.1 69.0 1.0 SG B:CYS52 2.5 71.2 1.0 CD2 B:HIS65 3.0 75.9 1.0 CE1 B:HIS65 3.1 76.8 1.0 C1A B:HEM1000 3.1 69.5 1.0 C1C B:HEM1000 3.1 69.0 1.0 C1B B:HEM1000 3.1 69.5 1.0 C1D B:HEM1000 3.1 68.8 1.0 C4B B:HEM1000 3.1 69.3 1.0 C4C B:HEM1000 3.1 68.9 1.0 C4D B:HEM1000 3.1 68.7 1.0 C4A B:HEM1000 3.1 69.6 1.0 CHA B:HEM1000 3.4 69.1 1.0 CHC B:HEM1000 3.4 69.1 1.0 CHB B:HEM1000 3.4 69.5 1.0 CHD B:HEM1000 3.4 68.9 1.0 CB B:CYS52 3.5 69.9 1.0 CG B:HIS65 4.1 75.4 1.0 ND1 B:HIS65 4.2 76.4 1.0 CA B:CYS52 4.2 69.7 1.0 C3C B:HEM1000 4.3 68.7 1.0 C3B B:HEM1000 4.3 69.6 1.0 C2C B:HEM1000 4.3 68.7 1.0 C2A B:HEM1000 4.3 70.0 1.0 C2B B:HEM1000 4.3 69.6 1.0 C3A B:HEM1000 4.3 69.7 1.0 C2D B:HEM1000 4.3 68.3 1.0 C3D B:HEM1000 4.3 68.1 1.0 NH1 B:ARG266 4.7 58.8 1.0 CD B:PRO64 5.0 77.4 1.0 CG B:PRO64 5.0 78.6 1.0

M.Petrosino, K.Zuhra, J.Kopec, A.Hutchin, C.Szabo, T.Majtan. H 2 S Biogenesis By Cystathionine Beta-Synthase: Mechanism of Inhibition By Aminooxyacetic Acid and Unexpected Role of Serine. Cell.Mol.Life Sci. V. 79 438 2022.
ISSN: ESSN 1420-9071
PubMed: 35864237
DOI: 10.1007/S00018-022-04479-9