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Iron in PDB 2vzw: X-Ray Structure of the Heme-Bound Gaf Domain of Sensory Histidine Kinase Dost of Mycobacterium Tuberculosis

Protein crystallography data

The structure of X-Ray Structure of the Heme-Bound Gaf Domain of Sensory Histidine Kinase Dost of Mycobacterium Tuberculosis, PDB code: 2vzw was solved by L.M.Podust, A.Ioanoviciu, P.R.Ortiz De Montellano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 88.05 / 2.30
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 87.924, 87.924, 66.760, 90.00, 90.00, 90.00
R / Rfree (%) 23.6 / 29

Iron Binding Sites:

The binding sites of Iron atom in the X-Ray Structure of the Heme-Bound Gaf Domain of Sensory Histidine Kinase Dost of Mycobacterium Tuberculosis (pdb code 2vzw). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the X-Ray Structure of the Heme-Bound Gaf Domain of Sensory Histidine Kinase Dost of Mycobacterium Tuberculosis, PDB code: 2vzw:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 2vzw

Go back to Iron Binding Sites List in 2vzw
Iron binding site 1 out of 2 in the X-Ray Structure of the Heme-Bound Gaf Domain of Sensory Histidine Kinase Dost of Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Structure of the Heme-Bound Gaf Domain of Sensory Histidine Kinase Dost of Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1206

b:39.3
occ:1.00
FE A:HEM1206 0.0 39.3 1.0
NC A:HEM1206 2.0 35.0 1.0
NA A:HEM1206 2.0 33.5 1.0
ND A:HEM1206 2.1 32.5 1.0
NE2 A:HIS147 2.1 41.6 1.0
NB A:HEM1206 2.2 33.5 1.0
CD2 A:HIS147 3.0 40.2 1.0
C4C A:HEM1206 3.0 33.2 1.0
C1C A:HEM1206 3.0 31.4 1.0
C1A A:HEM1206 3.0 34.9 1.0
C4A A:HEM1206 3.1 33.1 1.0
C4D A:HEM1206 3.1 36.6 1.0
C1D A:HEM1206 3.1 34.8 1.0
C4B A:HEM1206 3.1 32.5 1.0
C1B A:HEM1206 3.2 27.5 1.0
CE1 A:HIS147 3.2 41.8 1.0
CHC A:HEM1206 3.4 31.5 1.0
CHA A:HEM1206 3.4 34.0 1.0
CHD A:HEM1206 3.4 35.1 1.0
CHB A:HEM1206 3.5 32.5 1.0
O A:HOH2035 3.7 56.2 1.0
C3C A:HEM1206 4.2 33.0 1.0
CG A:HIS147 4.2 42.9 1.0
C2C A:HEM1206 4.2 31.8 1.0
C3A A:HEM1206 4.2 34.8 1.0
C2A A:HEM1206 4.3 34.2 1.0
ND1 A:HIS147 4.3 38.4 1.0
C3D A:HEM1206 4.3 33.4 1.0
C2D A:HEM1206 4.4 34.1 1.0
C3B A:HEM1206 4.4 29.9 1.0
C2B A:HEM1206 4.4 25.4 1.0

Iron binding site 2 out of 2 in 2vzw

Go back to Iron Binding Sites List in 2vzw
Iron binding site 2 out of 2 in the X-Ray Structure of the Heme-Bound Gaf Domain of Sensory Histidine Kinase Dost of Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of X-Ray Structure of the Heme-Bound Gaf Domain of Sensory Histidine Kinase Dost of Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1209

b:43.4
occ:1.00
FE B:HEM1209 0.0 43.4 1.0
NB B:HEM1209 2.0 40.1 1.0
NA B:HEM1209 2.0 41.0 1.0
NC B:HEM1209 2.1 42.7 1.0
NE2 B:HIS147 2.1 40.5 1.0
ND B:HEM1209 2.1 37.8 1.0
O2 B:OXY1210 2.6 44.3 1.0
CD2 B:HIS147 3.0 44.7 1.0
C4A B:HEM1209 3.0 41.8 1.0
C1B B:HEM1209 3.0 43.0 1.0
C4B B:HEM1209 3.1 40.5 1.0
C1A B:HEM1209 3.1 40.8 1.0
C4D B:HEM1209 3.1 39.3 1.0
C1C B:HEM1209 3.1 41.3 1.0
C4C B:HEM1209 3.1 40.9 1.0
C1D B:HEM1209 3.2 37.2 1.0
CE1 B:HIS147 3.2 43.1 1.0
CHB B:HEM1209 3.3 44.5 1.0
CHC B:HEM1209 3.4 42.3 1.0
CHA B:HEM1209 3.4 41.0 1.0
CHD B:HEM1209 3.5 40.2 1.0
O1 B:OXY1210 3.7 42.7 1.0
CG B:HIS147 4.2 39.8 1.0
ND1 B:HIS147 4.2 37.0 1.0
C3A B:HEM1209 4.2 42.0 1.0
C2A B:HEM1209 4.2 41.5 1.0
C2B B:HEM1209 4.3 43.8 1.0
C3B B:HEM1209 4.3 42.1 1.0
C2C B:HEM1209 4.3 43.1 1.0
C3C B:HEM1209 4.3 41.9 1.0
C3D B:HEM1209 4.3 39.5 1.0
C2D B:HEM1209 4.4 33.9 1.0
CG B:PRO113 4.9 45.8 1.0

Reference:

L.M.Podust, A.Ioanoviciu, P.R.Ortiz De Montellano. 2.3 A X-Ray Structure of the Heme-Bound Gaf Domain of Sensory Histidine Kinase Dost of Mycobacterium Tuberculosis. Biochemistry V. 47 12523 2008.
ISSN: ISSN 0006-2960
PubMed: 18980385
DOI: 10.1021/BI8012356
Page generated: Thu Jul 17 04:49:12 2025

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