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Zinc in PDB 6ba4: Crystal Structure of Myst Acetyltransferase Domain in Complex with Acetyl-Coa Cofactor

Enzymatic activity of Crystal Structure of Myst Acetyltransferase Domain in Complex with Acetyl-Coa Cofactor

All present enzymatic activity of Crystal Structure of Myst Acetyltransferase Domain in Complex with Acetyl-Coa Cofactor:
2.3.1.48;

Protein crystallography data

The structure of Crystal Structure of Myst Acetyltransferase Domain in Complex with Acetyl-Coa Cofactor, PDB code: 6ba4 was solved by S.J.Hermans, M.C.Chung, T.S.Peat, J.B.Baell, T.Thomas, M.W.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.68 / 1.95
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.363, 57.925, 120.045, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 21.3

Other elements in 6ba4:

The structure of Crystal Structure of Myst Acetyltransferase Domain in Complex with Acetyl-Coa Cofactor also contains other interesting chemical elements:

Sodium (Na) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Myst Acetyltransferase Domain in Complex with Acetyl-Coa Cofactor (pdb code 6ba4). 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 Crystal Structure of Myst Acetyltransferase Domain in Complex with Acetyl-Coa Cofactor, PDB code: 6ba4:

Zinc binding site 1 out of 1 in 6ba4

Go back to Zinc Binding Sites List in 6ba4
Zinc binding site 1 out of 1 in the Crystal Structure of Myst Acetyltransferase Domain in Complex with Acetyl-Coa Cofactor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Myst Acetyltransferase Domain in Complex with Acetyl-Coa Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn801

b:25.5
occ:1.00
NE2 A:HIS556 2.1 25.5 1.0
SG A:CYS543 2.2 24.4 1.0
SG A:CYS560 2.3 29.1 1.0
SG A:CYS540 2.3 22.7 1.0
CE1 A:HIS556 3.0 26.9 1.0
CB A:CYS540 3.1 18.5 1.0
CD2 A:HIS556 3.1 23.1 1.0
CB A:CYS560 3.2 24.8 1.0
CB A:CYS543 3.2 26.5 1.0
N A:CYS543 3.9 21.2 1.0
CA A:CYS543 4.1 23.2 1.0
ND1 A:HIS556 4.2 26.3 1.0
CG A:HIS556 4.2 28.1 1.0
O A:HOH1049 4.4 38.4 1.0
CA A:CYS560 4.5 30.1 1.0
CA A:CYS540 4.6 20.8 1.0
C A:CYS543 4.8 23.3 1.0
CB A:LYS545 4.9 22.9 1.0
N A:LEU544 4.9 22.0 1.0
C A:TYR542 5.0 26.5 1.0

Reference:

J.B.Baell, D.J.Leaver, S.J.Hermans, G.L.Kelly, M.S.Brennan, N.L.Downer, N.Nguyen, J.Wichmann, H.M.Mcrae, Y.Yang, B.Cleary, H.R.Lagiakos, S.Mieruszynski, G.Pacini, H.K.Vanyai, M.I.Bergamasco, R.E.May, B.K.Davey, K.J.Morgan, A.J.Sealey, B.Wang, N.Zamudio, S.Wilcox, A.L.Garnham, B.N.Sheikh, B.J.Aubrey, K.Doggett, M.C.Chung, M.De Silva, J.Bentley, P.Pilling, M.Hattarki, O.Dolezal, M.L.Dennis, H.Falk, B.Ren, S.A.Charman, K.L.White, J.Rautela, A.Newbold, E.D.Hawkins, R.W.Johnstone, N.D.Huntington, T.S.Peat, J.K.Heath, A.Strasser, M.W.Parker, G.K.Smyth, I.P.Street, B.J.Monahan, A.K.Voss, T.Thomas. Inhibitors of Histone Acetyltransferases KAT6A/B Induce Senescence and Arrest Tumour Growth. Nature V. 560 253 2018.
ISSN: ESSN 1476-4687
PubMed: 30069049
DOI: 10.1038/S41586-018-0387-5
Page generated: Wed Dec 16 11:31:43 2020

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