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Mercury in PDB 3qm0: Crystal Structure of RTT109-Ac-Coa Complex

Enzymatic activity of Crystal Structure of RTT109-Ac-Coa Complex

All present enzymatic activity of Crystal Structure of RTT109-Ac-Coa Complex:
2.3.1.48;

Protein crystallography data

The structure of Crystal Structure of RTT109-Ac-Coa Complex, PDB code: 3qm0 was solved by Y.Tang, R.Marmorstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 3.10
Space group F 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 233.791, 233.791, 233.791, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 25.8

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of RTT109-Ac-Coa Complex (pdb code 3qm0). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Crystal Structure of RTT109-Ac-Coa Complex, PDB code: 3qm0:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in 3qm0

Go back to Mercury Binding Sites List in 3qm0
Mercury binding site 1 out of 2 in the Crystal Structure of RTT109-Ac-Coa Complex


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of RTT109-Ac-Coa Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg800

b:44.5
occ:0.40
O A:CYS94 2.4 56.8 1.0
SG A:CYS94 2.4 51.5 1.0
O A:THR96 3.0 57.5 1.0
C A:CYS94 3.4 56.1 1.0
CB A:CYS94 3.7 53.8 1.0
N A:CYS94 3.7 52.2 1.0
CA A:CYS94 3.8 54.4 1.0
C A:THR96 4.1 57.9 1.0
N A:THR96 4.6 60.6 1.0
N A:ASN95 4.6 58.1 1.0
N A:TYR93 4.6 48.7 1.0
CA A:GLY92 4.7 47.1 1.0
C A:GLY92 4.8 47.9 1.0
C A:TYR93 4.9 50.8 1.0
CA A:ARG97 5.0 54.2 1.0
C A:ASN95 5.0 60.9 1.0
N A:ARG97 5.0 56.3 1.0

Mercury binding site 2 out of 2 in 3qm0

Go back to Mercury Binding Sites List in 3qm0
Mercury binding site 2 out of 2 in the Crystal Structure of RTT109-Ac-Coa Complex


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structure of RTT109-Ac-Coa Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg801

b:31.0
occ:0.30
SG A:CYS233 2.4 33.0 1.0
OE1 A:GLU109 2.7 42.4 1.0
O A:GLU232 2.8 24.1 1.0
CB A:CYS233 3.7 28.1 1.0
CD A:GLU109 3.8 39.6 1.0
C A:GLU232 3.8 25.9 1.0
CA A:CYS233 3.9 27.8 1.0
N A:CYS233 4.3 26.7 1.0
OE2 A:GLU109 4.5 42.4 1.0
CG A:GLU109 4.7 34.8 1.0
CB A:GLU232 4.9 28.2 1.0

Reference:

Y.Tang, M.A.Holbert, H.Wurtele, K.Meeth, W.Rocha, M.Gharib, E.Jiang, P.Thibault, A.Verrault, P.A.Cole, R.Marmorstein. Fungal RTT109 Histone Acetyltransferase Is An Unexpected Structural Homolog of Metazoan P300/Cbp. Nat.Struct.Mol.Biol. V. 15 738 2008.
ISSN: ISSN 1545-9993
PubMed: 18568037
DOI: 10.1038/NSMB.1448
Page generated: Wed Oct 28 18:42:58 2020

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