Iron in PDB 3vll: Crystal Structure Analysis of the SER305ALA Variant of Katg From Haloarcula Marismortui Complexes with Inhibitor Sha

All present enzymatic activity of Crystal Structure Analysis of the SER305ALA Variant of Katg From Haloarcula Marismortui Complexes with Inhibitor Sha:
1.11.1.21;

The structure of Crystal Structure Analysis of the SER305ALA Variant of Katg From Haloarcula Marismortui Complexes with Inhibitor Sha, PDB code: 3vll was solved by T.Sato, W.Higuchi, K.Yoshimatsu, T.Fujiwara, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.36 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	150.187, 76.320, 140.235, 90.00, 92.32, 90.00
R / Rfree (%)	24.7 / 27.1

The binding sites of Iron atom in the Crystal Structure Analysis of the SER305ALA Variant of Katg From Haloarcula Marismortui Complexes with Inhibitor Sha (pdb code 3vll). 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 Analysis of the SER305ALA Variant of Katg From Haloarcula Marismortui Complexes with Inhibitor Sha, PDB code: 3vll:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure Analysis of the SER305ALA Variant of Katg From Haloarcula Marismortui Complexes with Inhibitor Sha


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure Analysis of the SER305ALA Variant of Katg From Haloarcula Marismortui Complexes with Inhibitor Sha within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe800 b:20.4 occ:1.00 FE A:HEM800 0.0 20.4 1.0 NA A:HEM800 2.2 18.8 1.0 NB A:HEM800 2.2 18.7 1.0 ND A:HEM800 2.2 18.8 1.0 NC A:HEM800 2.2 16.1 1.0 NE2 A:HIS259 2.5 21.5 1.0 C1A A:HEM800 3.1 22.1 1.0 CHA A:HEM800 3.1 21.7 1.0 C4A A:HEM800 3.2 22.3 1.0 C4D A:HEM800 3.2 20.6 1.0 C1D A:HEM800 3.2 19.1 1.0 CHB A:HEM800 3.2 21.4 1.0 CHD A:HEM800 3.2 18.7 1.0 C1B A:HEM800 3.2 21.3 1.0 C1C A:HEM800 3.2 18.7 1.0 CHC A:HEM800 3.2 17.9 1.0 C4C A:HEM800 3.2 21.0 1.0 C4B A:HEM800 3.3 19.9 1.0 CD2 A:HIS259 3.3 19.5 1.0 CE1 A:HIS259 3.6 20.7 1.0 C2A A:HEM800 4.3 22.8 1.0 O9 A:SHA801 4.3 52.5 0.7 C3D A:HEM800 4.4 21.1 1.0 NE1 A:TRP95 4.4 24.4 1.0 C3A A:HEM800 4.4 23.8 1.0 C2C A:HEM800 4.5 16.0 1.0 C3C A:HEM800 4.5 18.9 1.0 C2D A:HEM800 4.5 19.5 1.0 C3B A:HEM800 4.5 19.8 1.0 CG A:HIS259 4.5 20.6 1.0 C2B A:HEM800 4.5 21.4 1.0 ND1 A:HIS259 4.6 21.1 1.0 CD1 A:TRP95 4.7 25.4 1.0 CH2 A:TRP311 4.8 22.4 1.0 N8 A:SHA801 4.9 52.4 0.7

Iron binding site 2 out of 2 in the Crystal Structure Analysis of the SER305ALA Variant of Katg From Haloarcula Marismortui Complexes with Inhibitor Sha


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure Analysis of the SER305ALA Variant of Katg From Haloarcula Marismortui Complexes with Inhibitor Sha within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe800 b:26.1 occ:1.00 FE B:HEM800 0.0 26.1 1.0 NA B:HEM800 2.2 27.4 1.0 ND B:HEM800 2.2 25.6 1.0 NE2 B:HIS259 2.3 27.3 1.0 NC B:HEM800 2.3 23.8 1.0 NB B:HEM800 2.4 28.6 1.0 CD2 B:HIS259 3.1 28.2 1.0 CHA B:HEM800 3.1 28.7 1.0 C4D B:HEM800 3.1 28.4 1.0 C1A B:HEM800 3.1 29.3 1.0 CHB B:HEM800 3.1 29.8 1.0 CHD B:HEM800 3.2 21.8 1.0 CHC B:HEM800 3.2 26.2 1.0 C1D B:HEM800 3.2 25.4 1.0 C4A B:HEM800 3.2 29.7 1.0 O9 B:SHA801 3.3 51.6 0.8 C4C B:HEM800 3.3 24.9 1.0 C1C B:HEM800 3.3 25.9 1.0 C1B B:HEM800 3.4 30.7 1.0 C4B B:HEM800 3.4 30.1 1.0 CE1 B:HIS259 3.4 28.2 1.0 N8 B:SHA801 3.8 51.3 0.8 O7 B:SHA801 4.0 49.8 0.8 C7 B:SHA801 4.2 51.4 0.8 CG B:HIS259 4.3 26.9 1.0 C3D B:HEM800 4.3 26.7 1.0 C2A B:HEM800 4.3 30.4 1.0 ND1 B:HIS259 4.4 28.1 1.0 C2D B:HEM800 4.4 24.8 1.0 C3A B:HEM800 4.5 30.5 1.0 NE1 B:TRP95 4.5 23.2 1.0 C2C B:HEM800 4.5 22.3 1.0 C3C B:HEM800 4.5 23.7 1.0 C3B B:HEM800 4.6 32.1 1.0 C2B B:HEM800 4.6 32.0 1.0 CD1 B:TRP95 4.6 25.2 1.0 CH2 B:TRP311 4.7 35.5 1.0

T.Sato, W.Higuchi, K.Yoshimatsu, T.Fujiwara. Crystal Structure and Kinetics Studies on SER305ALA Variant of Katg From Haloarcula Marismortui and Its Complexes with Inhibitor Sha To Be Published.