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Iron in PDB 3mz6: Crystal Structure of D101L FE2+ HDAC8 Complexed with M344

Enzymatic activity of Crystal Structure of D101L FE2+ HDAC8 Complexed with M344

All present enzymatic activity of Crystal Structure of D101L FE2+ HDAC8 Complexed with M344:
3.5.1.98;

Protein crystallography data

The structure of Crystal Structure of D101L FE2+ HDAC8 Complexed with M344, PDB code: 3mz6 was solved by D.P.Dowling, S.G.Gattis, C.A.Fierke, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 91.616, 87.561, 52.488, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 24.7

Other elements in 3mz6:

The structure of Crystal Structure of D101L FE2+ HDAC8 Complexed with M344 also contains other interesting chemical elements:

Potassium (K) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of D101L FE2+ HDAC8 Complexed with M344 (pdb code 3mz6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of D101L FE2+ HDAC8 Complexed with M344, PDB code: 3mz6:

Iron binding site 1 out of 1 in 3mz6

Go back to Iron Binding Sites List in 3mz6
Iron binding site 1 out of 1 in the Crystal Structure of D101L FE2+ HDAC8 Complexed with M344


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 D101L FE2+ HDAC8 Complexed with M344 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe400

b:16.9
occ:1.00
O4 A:B3N701 1.9 28.7 0.5
OD2 A:ASP267 1.9 20.8 1.0
OD2 A:ASP178 2.0 17.5 1.0
O A:HOH545 2.1 24.5 0.5
ND1 A:HIS180 2.1 15.5 1.0
O A:HOH397 2.2 10.4 0.5
O2 A:B3N701 2.6 22.1 0.5
N3 A:B3N701 2.7 26.3 0.5
CG A:ASP178 2.9 19.2 1.0
CG A:ASP267 3.0 23.2 1.0
CE1 A:HIS180 3.0 20.9 1.0
C1 A:B3N701 3.0 23.8 0.5
OD1 A:ASP178 3.2 14.8 1.0
CG A:HIS180 3.2 13.6 1.0
OD1 A:ASP267 3.4 17.5 1.0
CB A:HIS180 3.6 14.2 1.0
N A:HIS180 3.8 15.2 1.0
CA A:GLY304 4.1 24.5 1.0
NE2 A:HIS180 4.1 16.4 1.0
O A:HOH544 4.2 27.8 0.5
CD2 A:HIS180 4.3 16.0 1.0
CB A:ASP178 4.3 14.3 1.0
N A:LEU179 4.3 16.0 1.0
CB A:ASP267 4.3 20.7 1.0
CB A:LEU179 4.4 16.5 1.0
CA A:HIS180 4.4 15.6 1.0
C5 A:B3N701 4.4 25.9 0.5
NE2 A:HIS142 4.5 19.4 1.0
N A:GLY304 4.5 25.0 1.0
OH A:TYR306 4.6 30.7 1.0
CE1 A:TYR306 4.7 26.8 1.0
CA A:LEU179 4.7 16.3 1.0
C A:LEU179 4.7 17.1 1.0
CE1 A:HIS142 4.8 18.3 1.0
C6 A:B3N701 4.9 28.8 0.5
NE2 A:HIS143 5.0 19.9 1.0
C A:ASP178 5.0 16.6 1.0

Reference:

D.P.Dowling, S.G.Gattis, C.A.Fierke, D.W.Christianson. Structures of Metal-Substituted Human Histone Deacetylase 8 Provide Mechanistic Inferences on Biological Function. Biochemistry V. 49 5048 2010.
ISSN: ISSN 0006-2960
PubMed: 20545365
DOI: 10.1021/BI1005046
Page generated: Sun Aug 4 15:46:45 2024

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