Zinc in PDB 6sp0: Structure of ESCO2 Acetyltransferase in Complex with Coa

Protein crystallography data

The structure of Structure of ESCO2 Acetyltransferase in Complex with Coa, PDB code: 6sp0 was solved by I.De, V.Pena, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.62 / 1.77
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 52.680, 52.680, 107.470, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 19.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of ESCO2 Acetyltransferase in Complex with Coa (pdb code 6sp0). 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 Structure of ESCO2 Acetyltransferase in Complex with Coa, PDB code: 6sp0:

Zinc binding site 1 out of 1 in 6sp0

Go back to Zinc Binding Sites List in 6sp0
Zinc binding site 1 out of 1 in the Structure of ESCO2 Acetyltransferase in Complex with Coa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of ESCO2 Acetyltransferase in Complex with Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn602

b:37.4
occ:1.00
ND1 A:HIS408 2.0 35.0 1.0
NE2 A:HIS404 2.1 35.8 1.0
SG A:CYS386 2.3 39.5 1.0
SG A:CYS389 2.3 36.0 1.0
CE1 A:HIS408 2.9 44.8 1.0
CB A:CYS386 3.0 39.1 1.0
CG A:HIS408 3.0 36.2 1.0
CD2 A:HIS404 3.0 38.3 1.0
CE1 A:HIS404 3.1 37.6 1.0
CB A:CYS389 3.3 34.3 1.0
CB A:HIS408 3.4 30.8 1.0
N A:CYS389 3.8 37.8 1.0
NE2 A:HIS408 4.0 38.5 1.0
CD2 A:HIS408 4.1 37.1 1.0
CA A:CYS389 4.1 38.7 1.0
CA A:HIS408 4.2 31.6 1.0
ND1 A:HIS404 4.2 41.9 1.0
CG A:HIS404 4.2 37.2 1.0
CA A:CYS386 4.5 35.9 1.0
C A:SER388 4.8 46.3 1.0
C A:CYS389 4.8 31.5 1.0
N A:HIS408 4.9 30.6 1.0
O A:HIS404 5.0 35.0 1.0
C A:CYS386 5.0 42.3 1.0
CB A:MET391 5.0 31.0 1.0
N A:GLY390 5.0 31.5 1.0

Reference:

T.Ajam, I.De, N.Petkau, G.Whelan, V.Pena, G.Eichele. Alternative Catalytic Residues in the Active Site of Esco Acetyltransferases Sci Rep 2020.
ISSN: ESSN 2045-2322
DOI: 10.1038/S41598-020-66795-Z
Page generated: Wed Dec 16 12:49:14 2020

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