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Mercury in PDB 4qdo: Crystal Structure of AG85C Co-Crystallized with P-Chloromercuribenzoic Acid

Enzymatic activity of Crystal Structure of AG85C Co-Crystallized with P-Chloromercuribenzoic Acid

All present enzymatic activity of Crystal Structure of AG85C Co-Crystallized with P-Chloromercuribenzoic Acid:
2.3.1.122; 2.3.1.20;

Protein crystallography data

The structure of Crystal Structure of AG85C Co-Crystallized with P-Chloromercuribenzoic Acid, PDB code: 4qdo was solved by L.Favrot, D.H.Lajiness, D.R.Ronning, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.02 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.701, 67.988, 74.365, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 24

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of AG85C Co-Crystallized with P-Chloromercuribenzoic Acid (pdb code 4qdo). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Crystal Structure of AG85C Co-Crystallized with P-Chloromercuribenzoic Acid, PDB code: 4qdo:

Mercury binding site 1 out of 1 in 4qdo

Go back to Mercury Binding Sites List in 4qdo
Mercury binding site 1 out of 1 in the Crystal Structure of AG85C Co-Crystallized with P-Chloromercuribenzoic Acid


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 AG85C Co-Crystallized with P-Chloromercuribenzoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg209

b:43.8
occ:1.00
HG A:31Q209 0.0 43.8 1.0
C07 A:31Q209 2.2 35.9 1.0
SG A:31Q209 2.6 45.6 1.0
O A:31Q209 3.0 21.9 1.0
C06 A:31Q209 3.0 39.5 1.0
O A:GLY210 3.1 41.6 1.0
C15 A:31Q209 3.2 36.7 1.0
C A:31Q209 3.3 28.2 1.0
CB A:31Q209 3.5 34.9 1.0
C A:GLY210 3.6 38.2 1.0
CD1 A:PHE254 3.8 40.4 1.0
N A:GLY210 3.9 30.6 1.0
CA A:31Q209 3.9 32.8 1.0
CA A:GLY210 4.2 36.5 1.0
CE1 A:PHE254 4.2 42.5 1.0
C05 A:31Q209 4.4 36.4 1.0
N A:ASN211 4.4 39.5 1.0
C16 A:31Q209 4.5 37.1 0.8
CD1 A:LEU232 4.5 38.2 1.0
CG A:PHE254 4.7 31.8 1.0
CA A:ASN211 4.8 42.3 1.0
CB A:PHE254 4.9 27.1 1.0
C04 A:31Q209 4.9 40.6 0.6

Reference:

L.Favrot, D.H.Lajiness, D.R.Ronning. Inactivation of the Mycobacterium Tuberculosis Antigen 85 Complex By Covalent, Allosteric Inhibitors. J.Biol.Chem. V. 289 25031 2014.
ISSN: ISSN 0021-9258
PubMed: 25028518
DOI: 10.1074/JBC.M114.582445
Page generated: Sun Dec 13 19:11:52 2020

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