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Zinc in PDB 4bkx: The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex

Enzymatic activity of The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex

All present enzymatic activity of The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex:
3.5.1.98;

Protein crystallography data

The structure of The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex, PDB code: 4bkx was solved by C.J.Millard, P.J.Watson, I.Celardo, Y.Gordiyenko, S.M.Cowley, C.V.Robinson, L.Fairall, J.W.R.Schwabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 76.75 / 3.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 108.199, 108.199, 133.164, 90.00, 90.00, 120.00
R / Rfree (%) 21.084 / 26.149

Other elements in 4bkx:

The structure of The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex also contains other interesting chemical elements:

Potassium (K) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex (pdb code 4bkx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex, PDB code: 4bkx:

Zinc binding site 1 out of 1 in 4bkx

Go back to Zinc Binding Sites List in 4bkx
Zinc binding site 1 out of 1 in the The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn600

b:40.8
occ:1.00
 OD2 B:ASP264 1.9 40.5 1.0
OD1 B:ASP176 2.0 42.3 1.0
ND1 B:HIS178 2.3 44.5 1.0
OXT B:ACT601 2.3 35.2 1.0
O B:ACT601 2.5 34.4 1.0
C B:ACT601 2.7 34.9 1.0
CG B:ASP176 2.8 42.2 1.0
OD2 B:ASP176 2.9 42.0 1.0
CG B:ASP264 3.0 40.8 1.0
CG B:HIS178 3.2 44.3 1.0
CE1 B:HIS178 3.2 45.1 1.0
OD1 B:ASP264 3.3 41.7 1.0
CB B:HIS178 3.5 44.0 1.0
N B:HIS178 3.8 43.4 1.0
CA B:GLY301 4.1 38.7 1.0
CG2 B:ILE177 4.2 42.5 1.0
CH3 B:ACT601 4.2 34.9 1.0
CB B:ASP176 4.2 42.3 1.0
CA B:HIS178 4.2 44.0 1.0
NE2 B:HIS140 4.3 49.5 1.0
CB B:ASP264 4.3 40.3 1.0
NE2 B:HIS178 4.3 44.5 1.0
CD2 B:HIS178 4.4 44.7 1.0
N B:ILE177 4.4 42.3 1.0
NE2 B:HIS141 4.4 58.0 1.0
N B:GLY301 4.5 38.5 1.0
CE2 B:TYR303 4.6 42.5 1.0
OH B:TYR303 4.6 41.8 1.0
C B:ILE177 4.8 42.8 1.0
C B:ASP176 4.8 43.0 1.0
CA B:ASP176 4.9 43.3 1.0
CE1 B:HIS140 5.0 49.9 1.0
CA B:ILE177 5.0 42.2 1.0
O B:HIS178 5.0 44.2 1.0

Reference:

C.J.Millard, P.J.Watson, I.Celardo, Y.Gordiyenko, S.M.Cowley, C.V.Robinson, L.Fairall, J.W.R.Schwabe. Class I Hdacs Share A Common Mechanism of Regulation By Inositol Phosphates. Mol.Cell V. 51 57 2013.
ISSN: ISSN 1097-2765
PubMed: 23791785
DOI: 10.1016/J.MOLCEL.2013.05.020
Page generated: Sat Oct 26 19:49:39 2024

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