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Iron in PDB 3uw8: Crystal Structure Analysis of the SER305THR Variants of Katg From Haloarcula Marismortui

Enzymatic activity of Crystal Structure Analysis of the SER305THR Variants of Katg From Haloarcula Marismortui

All present enzymatic activity of Crystal Structure Analysis of the SER305THR Variants of Katg From Haloarcula Marismortui:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure Analysis of the SER305THR Variants of Katg From Haloarcula Marismortui, PDB code: 3uw8 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) 24.81 / 2.35
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 315.410, 81.120, 75.020, 90.00, 99.84, 90.00
R / Rfree (%) 25.7 / 30.9

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure Analysis of the SER305THR Variants of Katg From Haloarcula Marismortui (pdb code 3uw8). 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 SER305THR Variants of Katg From Haloarcula Marismortui, PDB code: 3uw8:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 3uw8

Go back to Iron Binding Sites List in 3uw8
Iron binding site 1 out of 2 in the Crystal Structure Analysis of the SER305THR Variants of Katg From Haloarcula Marismortui


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 SER305THR Variants of Katg From Haloarcula Marismortui within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe800

b:30.3
occ:1.00
FE A:HEM800 0.0 30.3 1.0
NE2 A:HIS259 2.2 20.3 1.0
NA A:HEM800 2.2 29.9 1.0
NB A:HEM800 2.3 28.8 1.0
ND A:HEM800 2.3 30.1 1.0
NC A:HEM800 2.4 28.0 1.0
CD2 A:HIS259 3.0 22.2 1.0
CHD A:HEM800 3.0 25.8 1.0
CHA A:HEM800 3.1 32.9 1.0
CHB A:HEM800 3.1 26.8 1.0
CHC A:HEM800 3.1 31.1 1.0
C4A A:HEM800 3.2 28.2 1.0
C1A A:HEM800 3.2 31.8 1.0
CE1 A:HIS259 3.2 22.8 1.0
C4D A:HEM800 3.3 30.5 1.0
C1B A:HEM800 3.3 27.9 1.0
C1D A:HEM800 3.3 27.7 1.0
C1C A:HEM800 3.3 27.7 1.0
C4B A:HEM800 3.3 30.9 1.0
C4C A:HEM800 3.3 26.1 1.0
O A:HOH798 4.1 45.2 1.0
CG A:HIS259 4.2 21.8 1.0
ND1 A:HIS259 4.3 20.5 1.0
C2A A:HEM800 4.4 30.9 1.0
NE1 A:TRP95 4.4 32.1 1.0
C3D A:HEM800 4.4 29.6 1.0
C3C A:HEM800 4.5 25.3 1.0
C2C A:HEM800 4.5 24.7 1.0
C3A A:HEM800 4.5 30.8 1.0
C2D A:HEM800 4.5 28.5 1.0
C2B A:HEM800 4.5 28.2 1.0
C3B A:HEM800 4.5 28.5 1.0
CH2 A:TRP311 4.6 19.1 1.0
CZ2 A:TRP311 4.7 22.7 1.0
CD1 A:TRP95 4.9 32.7 1.0

Iron binding site 2 out of 2 in 3uw8

Go back to Iron Binding Sites List in 3uw8
Iron binding site 2 out of 2 in the Crystal Structure Analysis of the SER305THR Variants of Katg From Haloarcula Marismortui


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 SER305THR Variants of Katg From Haloarcula Marismortui within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe800

b:53.0
occ:1.00
FE B:HEM800 0.0 53.0 1.0
NA B:HEM800 2.1 50.2 1.0
NB B:HEM800 2.2 49.6 1.0
ND B:HEM800 2.3 49.5 1.0
NC B:HEM800 2.3 48.8 1.0
NE2 B:HIS259 2.5 56.4 1.0
CHB B:HEM800 3.0 50.3 1.0
CHA B:HEM800 3.0 51.2 1.0
CHC B:HEM800 3.1 50.0 1.0
C4A B:HEM800 3.1 50.5 1.0
C1B B:HEM800 3.1 50.1 1.0
C1A B:HEM800 3.1 51.2 1.0
C4B B:HEM800 3.2 50.3 1.0
CD2 B:HIS259 3.3 54.4 1.0
C4D B:HEM800 3.3 50.3 1.0
C1C B:HEM800 3.3 49.3 1.0
CHD B:HEM800 3.3 48.0 1.0
C1D B:HEM800 3.4 49.1 1.0
C4C B:HEM800 3.4 48.3 1.0
CE1 B:HIS259 3.6 56.0 1.0
C2A B:HEM800 4.3 51.9 1.0
C3A B:HEM800 4.4 51.9 1.0
NE1 B:TRP95 4.4 50.6 1.0
C3B B:HEM800 4.4 49.9 1.0
CD1 B:TRP95 4.4 50.2 1.0
C2B B:HEM800 4.4 50.0 1.0
C2C B:HEM800 4.5 50.1 1.0
CG B:HIS259 4.5 55.3 1.0
C3D B:HEM800 4.5 51.0 1.0
C3C B:HEM800 4.6 48.7 1.0
C2D B:HEM800 4.6 50.6 1.0
CH2 B:TRP311 4.6 60.1 1.0
ND1 B:HIS259 4.6 56.4 1.0
CZ2 B:TRP311 4.9 59.9 1.0

Reference:

T.Sato, W.Higuchi, K.Yoshimatsu, T.Fujiwara. Catalatic Implication Guided By Structure, Kinetics and Theoretical Studies on SER305THR and ARG409LEU Variants of Hmkatg To Be Published.
Page generated: Sun Aug 4 21:31:57 2024

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