Iron in PDB 3t7v: Crystal Structure of Methylornithine Synthase (Pylb)

All present enzymatic activity of Crystal Structure of Methylornithine Synthase (Pylb):
2.8.1.6;

The structure of Crystal Structure of Methylornithine Synthase (Pylb), PDB code: 3t7v was solved by F.Quitterer, A.List, W.Eisenreich, A.Bacher, M.Groll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.50
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	77.020, 77.020, 104.950, 90.00, 90.00, 120.00
R / Rfree (%)	12.9 / 16.5

The binding sites of Iron atom in the Crystal Structure of Methylornithine Synthase (Pylb) (pdb code 3t7v). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Methylornithine Synthase (Pylb), PDB code: 3t7v:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Methylornithine Synthase (Pylb)


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 Methylornithine Synthase (Pylb) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe991 b:13.9 occ:1.00 FE1 A:SF4991 0.0 13.9 1.0 O A:SAM992 2.2 15.5 1.0 N A:SAM992 2.2 18.2 1.0 S2 A:SF4991 2.3 12.4 1.0 S3 A:SF4991 2.3 12.8 1.0 S4 A:SF4991 2.4 12.5 1.0 FE2 A:SF4991 2.8 12.5 1.0 FE4 A:SF4991 2.8 12.8 1.0 FE3 A:SF4991 2.8 12.7 1.0 C A:SAM992 2.9 15.1 1.0 CA A:SAM992 3.0 16.6 1.0 SD A:SAM992 3.2 22.6 0.5 CG A:SAM992 3.3 25.2 0.5 CB A:SAM992 3.6 20.9 1.0 CG A:SAM992 3.8 22.4 0.5 S1 A:SF4991 4.0 13.3 1.0 NH2 A:ARG182 4.2 16.1 1.0 OXT A:SAM992 4.2 14.4 1.0 CE A:SAM992 4.3 32.5 0.5 O A:HOH368 4.3 15.3 1.0 C5' A:SAM992 4.4 26.8 0.5 NH1 A:ARG182 4.4 12.8 1.0 SD A:SAM992 4.6 28.5 0.5 SG A:CYS71 4.7 11.5 1.0 CZ A:ARG182 4.8 13.4 1.0 C5' A:SAM992 4.9 23.9 0.5 CA A:GLY116 4.9 11.7 1.0 SG A:CYS75 5.0 12.8 1.0 SG A:CYS78 5.0 12.1 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Methylornithine Synthase (Pylb)


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 Methylornithine Synthase (Pylb) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe991 b:12.5 occ:1.00 FE2 A:SF4991 0.0 12.5 1.0 S1 A:SF4991 2.2 13.3 1.0 S4 A:SF4991 2.3 12.5 1.0 SG A:CYS71 2.3 11.5 1.0 S3 A:SF4991 2.3 12.8 1.0 FE3 A:SF4991 2.7 12.7 1.0 FE4 A:SF4991 2.7 12.8 1.0 FE1 A:SF4991 2.8 13.9 1.0 CB A:CYS71 3.4 12.3 1.0 S2 A:SF4991 3.8 12.4 1.0 N A:SAM992 3.9 18.2 1.0 CB A:ASN73 4.1 13.7 1.0 CA A:GLY116 4.5 11.7 1.0 N A:GLU117 4.5 11.0 1.0 CA A:CYS71 4.7 12.6 1.0 O A:SAM992 4.7 15.5 1.0 SG A:CYS75 4.8 12.8 1.0 SG A:CYS78 4.8 12.1 1.0 O A:ASN73 4.8 16.7 1.0 N A:ASN73 4.8 13.5 1.0 O A:TYR80 4.9 12.1 1.0 CA A:ASN73 4.9 12.7 1.0 OD1 A:ASN73 5.0 20.3 1.0 C A:ASN73 5.0 13.2 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Methylornithine Synthase (Pylb)


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 Methylornithine Synthase (Pylb) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe991 b:12.7 occ:1.00 FE3 A:SF4991 0.0 12.7 1.0 S4 A:SF4991 2.2 12.5 1.0 S2 A:SF4991 2.3 12.4 1.0 S1 A:SF4991 2.3 13.3 1.0 SG A:CYS78 2.3 12.1 1.0 FE4 A:SF4991 2.6 12.8 1.0 FE2 A:SF4991 2.7 12.5 1.0 FE1 A:SF4991 2.8 13.9 1.0 CB A:CYS78 3.1 12.2 1.0 S3 A:SF4991 3.9 12.8 1.0 SD A:SAM992 4.3 22.6 0.5 CE A:SAM992 4.4 32.5 0.5 CB A:TYR80 4.5 12.5 1.0 CA A:CYS78 4.6 11.5 1.0 SG A:CYS75 4.6 12.8 1.0 CB A:CYS75 4.7 11.7 1.0 N A:SAM992 4.7 18.2 1.0 N A:ASN81 4.7 11.4 1.0 C A:TYR80 4.7 11.5 1.0 O A:SAM992 4.8 15.5 1.0 SG A:CYS71 4.8 11.5 1.0 N A:TYR80 4.9 11.3 1.0 CA A:TYR80 5.0 11.8 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Methylornithine Synthase (Pylb)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Methylornithine Synthase (Pylb) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe991 b:12.8 occ:1.00 FE4 A:SF4991 0.0 12.8 1.0 S3 A:SF4991 2.2 12.8 1.0 S1 A:SF4991 2.3 13.3 1.0 S2 A:SF4991 2.3 12.4 1.0 SG A:CYS75 2.3 12.8 1.0 FE3 A:SF4991 2.6 12.7 1.0 FE2 A:SF4991 2.7 12.5 1.0 FE1 A:SF4991 2.8 13.9 1.0 CB A:CYS75 3.2 11.7 1.0 NH1 A:ARG182 3.7 12.8 1.0 S4 A:SF4991 3.8 12.5 1.0 O A:SAM992 3.9 15.5 1.0 N A:CYS75 4.4 11.9 1.0 CZ A:ARG182 4.4 13.4 1.0 NH2 A:ARG182 4.4 16.1 1.0 CB A:CYS78 4.4 12.2 1.0 CB A:ASN73 4.4 13.7 1.0 CA A:CYS75 4.4 11.4 1.0 SG A:CYS78 4.6 12.1 1.0 SG A:CYS71 4.7 11.5 1.0 CZ A:PHE77 4.7 13.8 1.0 NE2 A:GLN185 4.8 17.9 1.0 N A:SAM992 4.8 18.2 1.0 OD1 A:ASN73 4.9 20.3 1.0 CE1 A:PHE77 4.9 14.3 1.0

F.Quitterer, A.List, W.Eisenreich, A.Bacher, M.Groll. Crystal Structure of Methylornithine Synthase (Pylb): Insights Into the Pyrrolysine Biosynthesis. Angew.Chem.Int.Ed.Engl. V. 51 1339 2012.
ISSN: ISSN 1433-7851
PubMed: 22095926
DOI: 10.1002/ANIE.201106765