Iron in PDB 4pcu: Crystal Structure of DELTA516-525 E201S Human Cystathionine Beta- Synthase with Adomet

All present enzymatic activity of Crystal Structure of DELTA516-525 E201S Human Cystathionine Beta- Synthase with Adomet:
4.2.1.22;

The structure of Crystal Structure of DELTA516-525 E201S Human Cystathionine Beta- Synthase with Adomet, PDB code: 4pcu was solved by J.Ereno-Orbea, 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)	40.81 / 3.58
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	141.354, 141.354, 108.528, 90.00, 90.00, 120.00
R / Rfree (%)	25.7 / 27.7

The binding sites of Iron atom in the Crystal Structure of DELTA516-525 E201S Human Cystathionine Beta- Synthase with Adomet (pdb code 4pcu). 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 E201S Human Cystathionine Beta- Synthase with Adomet, PDB code: 4pcu:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of DELTA516-525 E201S Human Cystathionine Beta- Synthase with Adomet


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 E201S Human Cystathionine Beta- Synthase with Adomet within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:89.6 occ:1.00 FE A:HEM601 0.0 89.6 1.0 ND A:HEM601 2.0 89.1 1.0 NB A:HEM601 2.0 90.3 1.0 NA A:HEM601 2.0 92.2 1.0 NC A:HEM601 2.0 87.1 1.0 NE2 A:HIS65 2.2 91.3 1.0 SG A:CYS52 2.3 87.9 1.0 CE1 A:HIS65 3.0 91.1 1.0 C1D A:HEM601 3.0 87.7 1.0 C4D A:HEM601 3.0 90.5 1.0 C4B A:HEM601 3.0 89.2 1.0 C1B A:HEM601 3.0 92.0 1.0 C4A A:HEM601 3.1 93.7 1.0 C1A A:HEM601 3.1 93.1 1.0 C1C A:HEM601 3.1 86.5 1.0 C4C A:HEM601 3.1 85.9 1.0 CD2 A:HIS65 3.3 90.4 1.0 CHA A:HEM601 3.4 92.3 1.0 CHD A:HEM601 3.4 86.2 1.0 CHC A:HEM601 3.4 87.5 1.0 CHB A:HEM601 3.4 93.6 1.0 CB A:CYS52 3.5 89.0 1.0 ND1 A:HIS65 4.2 90.2 1.0 C3D A:HEM601 4.3 90.0 1.0 C2D A:HEM601 4.3 88.1 1.0 C3A A:HEM601 4.3 95.5 1.0 C2B A:HEM601 4.3 92.2 1.0 C3B A:HEM601 4.3 90.5 1.0 C2A A:HEM601 4.3 95.2 1.0 C2C A:HEM601 4.3 84.8 1.0 CA A:CYS52 4.3 91.2 1.0 C3C A:HEM601 4.3 84.5 1.0 CG A:HIS65 4.3 89.7 1.0 CB A:TRP54 4.6 85.9 1.0 NH1 A:ARG266 4.7 87.7 1.0 N A:THR53 4.8 90.2 1.0 N A:TRP54 4.8 89.2 1.0 C A:CYS52 5.0 92.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of DELTA516-525 E201S Human Cystathionine Beta- Synthase with Adomet


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 E201S Human Cystathionine Beta- Synthase with Adomet within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:87.5 occ:1.00 FE B:HEM601 0.0 87.5 1.0 NB B:HEM601 2.0 87.6 1.0 NC B:HEM601 2.0 85.1 1.0 ND B:HEM601 2.0 87.7 1.0 NA B:HEM601 2.0 90.2 1.0 NE2 B:HIS65 2.2 88.1 1.0 SG B:CYS52 2.3 86.7 1.0 C4B B:HEM601 3.0 86.4 1.0 C1B B:HEM601 3.0 89.2 1.0 C1C B:HEM601 3.0 84.2 1.0 C4C B:HEM601 3.0 84.2 1.0 C1D B:HEM601 3.1 86.4 1.0 C4A B:HEM601 3.1 91.4 1.0 C4D B:HEM601 3.1 89.3 1.0 CE1 B:HIS65 3.1 88.2 1.0 C1A B:HEM601 3.1 91.4 1.0 CD2 B:HIS65 3.2 87.1 1.0 CHC B:HEM601 3.4 84.8 1.0 CHB B:HEM601 3.4 90.9 1.0 CHD B:HEM601 3.4 84.8 1.0 CHA B:HEM601 3.4 90.9 1.0 CB B:CYS52 3.6 88.4 1.0 ND1 B:HIS65 4.2 87.2 1.0 C2B B:HEM601 4.3 88.9 1.0 C3B B:HEM601 4.3 87.2 1.0 C2C B:HEM601 4.3 82.6 1.0 C3C B:HEM601 4.3 82.6 1.0 CA B:CYS52 4.3 90.5 1.0 C3A B:HEM601 4.3 93.3 1.0 C3D B:HEM601 4.3 89.1 1.0 C2D B:HEM601 4.3 87.2 1.0 C2A B:HEM601 4.3 93.4 1.0 CG B:HIS65 4.3 86.5 1.0 NH1 B:ARG266 4.7 84.6 1.0 CB B:TRP54 4.8 87.0 1.0 N B:THR53 4.9 89.5 1.0 N B:TRP54 5.0 90.4 1.0

J.Ereno-Orbea, T.Majtan, I.Oyenarte, J.P.Kraus, L.A.Martinez-Cruz. Structural Insight Into the Molecular Mechanism of Allosteric Activation of Human Cystathionine Beta-Synthase By S-Adenosylmethionine. Proc.Natl.Acad.Sci.Usa V. 111 E3845 2014.
ISSN: ESSN 1091-6490
PubMed: 25197074
DOI: 10.1073/PNAS.1414545111