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Iron in PDB 2y79: Structure of the First Gaf Domain E87A Mutant of Mycobacterium Tuberculosis Doss

Enzymatic activity of Structure of the First Gaf Domain E87A Mutant of Mycobacterium Tuberculosis Doss

All present enzymatic activity of Structure of the First Gaf Domain E87A Mutant of Mycobacterium Tuberculosis Doss:
2.7.13.3;

Protein crystallography data

The structure of Structure of the First Gaf Domain E87A Mutant of Mycobacterium Tuberculosis Doss, PDB code: 2y79 was solved by H.Y.Cho, H.J.Cho, B.S.Kang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.39 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 35.932, 86.913, 100.973, 90.00, 90.00, 90.00
R / Rfree (%) 19.658 / 24.808

Other elements in 2y79:

The structure of Structure of the First Gaf Domain E87A Mutant of Mycobacterium Tuberculosis Doss also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of the First Gaf Domain E87A Mutant of Mycobacterium Tuberculosis Doss (pdb code 2y79). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of the First Gaf Domain E87A Mutant of Mycobacterium Tuberculosis Doss, PDB code: 2y79:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 2y79

Go back to Iron Binding Sites List in 2y79
Iron binding site 1 out of 2 in the Structure of the First Gaf Domain E87A Mutant of Mycobacterium Tuberculosis Doss


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the First Gaf Domain E87A Mutant of Mycobacterium Tuberculosis Doss within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:15.4
occ:1.00
FE A:HEM500 0.0 15.4 1.0
NB A:HEM500 2.0 14.0 1.0
NA A:HEM500 2.0 14.3 1.0
NC A:HEM500 2.1 13.8 1.0
ND A:HEM500 2.1 14.5 1.0
NE2 A:HIS149 2.2 14.2 1.0
O A:HOH2111 2.4 22.3 1.0
CD2 A:HIS149 3.0 15.6 1.0
C4B A:HEM500 3.0 12.7 1.0
C1B A:HEM500 3.0 12.4 1.0
C1A A:HEM500 3.1 13.8 1.0
C4A A:HEM500 3.1 14.0 1.0
C1C A:HEM500 3.1 14.7 1.0
C4C A:HEM500 3.1 11.6 1.0
C1D A:HEM500 3.1 13.4 1.0
C4D A:HEM500 3.1 14.1 1.0
CE1 A:HIS149 3.2 15.3 1.0
CHC A:HEM500 3.4 14.6 1.0
CHB A:HEM500 3.4 13.6 1.0
CHA A:HEM500 3.4 12.8 1.0
CHD A:HEM500 3.4 13.9 1.0
CG A:HIS149 4.2 15.8 1.0
C2B A:HEM500 4.3 11.3 1.0
ND1 A:HIS149 4.3 14.1 1.0
C3B A:HEM500 4.3 13.2 1.0
C2A A:HEM500 4.3 15.1 1.0
C3A A:HEM500 4.3 14.7 1.0
C2C A:HEM500 4.3 15.3 1.0
C3C A:HEM500 4.3 14.5 1.0
C3D A:HEM500 4.3 14.4 1.0
C2D A:HEM500 4.3 13.1 1.0
O A:HOH2109 4.4 32.0 1.0
CB A:PRO115 4.9 16.8 1.0

Iron binding site 2 out of 2 in 2y79

Go back to Iron Binding Sites List in 2y79
Iron binding site 2 out of 2 in the Structure of the First Gaf Domain E87A Mutant of Mycobacterium Tuberculosis Doss


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the First Gaf Domain E87A Mutant of Mycobacterium Tuberculosis Doss within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:16.1
occ:1.00
FE B:HEM502 0.0 16.1 1.0
NB B:HEM502 2.0 15.4 1.0
NA B:HEM502 2.0 14.6 1.0
NC B:HEM502 2.0 14.7 1.0
NE2 B:HIS149 2.1 13.2 1.0
ND B:HEM502 2.2 16.1 1.0
O B:HOH2104 2.4 24.8 1.0
C1B B:HEM502 3.0 14.4 1.0
C4B B:HEM502 3.0 16.7 1.0
C4A B:HEM502 3.0 17.6 1.0
C4C B:HEM502 3.0 16.9 1.0
CE1 B:HIS149 3.0 13.7 1.0
C1A B:HEM502 3.1 20.7 1.0
C1C B:HEM502 3.1 18.8 1.0
CD2 B:HIS149 3.1 12.3 1.0
C1D B:HEM502 3.1 15.8 1.0
C4D B:HEM502 3.2 16.5 1.0
CHD B:HEM502 3.4 16.4 1.0
CHB B:HEM502 3.4 16.9 1.0
CHC B:HEM502 3.4 16.3 1.0
CHA B:HEM502 3.5 17.9 1.0
ND1 B:HIS149 4.2 16.6 1.0
CG B:HIS149 4.2 14.1 1.0
C3B B:HEM502 4.2 16.9 1.0
C2B B:HEM502 4.2 14.3 1.0
C3A B:HEM502 4.2 19.4 1.0
C2A B:HEM502 4.3 20.3 1.0
C3C B:HEM502 4.3 16.4 1.0
C2C B:HEM502 4.3 16.2 1.0
C2D B:HEM502 4.4 16.0 1.0
C3D B:HEM502 4.4 17.1 1.0
O B:HOH2106 4.7 29.6 1.0

Reference:

H.Y.Cho, H.J.Cho, M.H.Kim, B.S.Kang. Blockage of the Channel to Heme By the E87 Side Chain in the Gaf Domain of Mycobacterium Tuberculosis Doss Confers the Unique Sensitivity of Doss to Oxygen. Febs Lett. V. 585 1873 2011.
ISSN: ISSN 0014-5793
PubMed: 21536032
DOI: 10.1016/J.FEBSLET.2011.04.050
Page generated: Sun Dec 13 14:57:35 2020

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