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Cobalt in PDB 3mz7: Crystal Structure of D101L CO2+ HDAC8 Complexed with M344

Enzymatic activity of Crystal Structure of D101L CO2+ HDAC8 Complexed with M344

All present enzymatic activity of Crystal Structure of D101L CO2+ HDAC8 Complexed with M344:
3.5.1.98;

Protein crystallography data

The structure of Crystal Structure of D101L CO2+ HDAC8 Complexed with M344, PDB code: 3mz7 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) 45.15 / 1.90
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 91.799, 88.431, 52.503, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 25.6

Other elements in 3mz7:

The structure of Crystal Structure of D101L CO2+ HDAC8 Complexed with M344 also contains other interesting chemical elements:

Potassium (K) 2 atoms

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of D101L CO2+ HDAC8 Complexed with M344 (pdb code 3mz7). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of D101L CO2+ HDAC8 Complexed with M344, PDB code: 3mz7:

Cobalt binding site 1 out of 1 in 3mz7

Go back to Cobalt Binding Sites List in 3mz7
Cobalt binding site 1 out of 1 in the Crystal Structure of D101L CO2+ HDAC8 Complexed with M344


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of D101L CO2+ HDAC8 Complexed with M344 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co390

b:25.1
occ:1.00
O4 A:B3N701 1.8 13.5 0.5
OD2 A:ASP267 2.0 23.7 1.0
OD2 A:ASP178 2.0 21.7 1.0
O A:HOH537 2.1 19.2 0.5
ND1 A:HIS180 2.1 18.7 1.0
O2 A:B3N701 2.4 19.4 0.5
N3 A:B3N701 2.5 18.6 0.5
O A:HOH538 2.7 31.9 0.2
C1 A:B3N701 2.8 19.4 0.5
CG A:ASP178 2.9 24.0 1.0
CE1 A:HIS180 3.0 24.7 1.0
CG A:ASP267 3.0 25.0 1.0
OD1 A:ASP178 3.1 20.9 1.0
CG A:HIS180 3.2 17.6 1.0
OD1 A:ASP267 3.4 24.4 1.0
CB A:HIS180 3.6 20.0 1.0
N A:HIS180 3.9 22.2 1.0
CA A:GLY304 4.1 25.4 1.0
NE2 A:HIS180 4.2 23.1 1.0
C5 A:B3N701 4.3 22.8 0.5
CD2 A:HIS180 4.3 20.3 1.0
CB A:ASP178 4.3 20.2 1.0
O3 A:GOL706 4.3 43.8 0.2
N A:LEU179 4.3 20.9 1.0
NE2 A:HIS142 4.4 22.9 1.0
CB A:ASP267 4.4 26.3 1.0
OH A:TYR306 4.4 30.6 1.0
CA A:HIS180 4.4 22.5 1.0
N A:GLY304 4.4 26.2 1.0
CB A:LEU179 4.5 21.2 1.0
CE1 A:HIS142 4.7 25.3 1.0
C A:LEU179 4.8 24.4 1.0
CA A:LEU179 4.8 21.6 1.0
C6 A:B3N701 4.8 26.2 0.5
CE1 A:TYR306 4.8 28.8 1.0
NE2 A:HIS143 4.9 25.5 1.0
C A:ASP178 5.0 22.7 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 Dec 13 10:41:35 2020

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