Atomistry » Mercury » PDB 1rsv-1yp2 » 1sdn
Atomistry »
  Mercury »
    PDB 1rsv-1yp2 »
      1sdn »

Mercury in PDB 1sdn: Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury

Enzymatic activity of Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury

All present enzymatic activity of Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury:
3.4.16.4;

Protein crystallography data

The structure of Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury, PDB code: 1sdn was solved by G.Nicola, R.A.Nicholas, C.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.50
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 50.700, 50.700, 140.300, 90.00, 90.00, 120.00
R / Rfree (%) 17.1 / 24.1

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury (pdb code 1sdn). 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 A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury, PDB code: 1sdn:

Mercury binding site 1 out of 1 in 1sdn

Go back to Mercury Binding Sites List in 1sdn
Mercury binding site 1 out of 1 in the Crystal Structure of A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury


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 A Deacylation-Defective Mutant of Penicillin-Binding Protein 5 Modified By Mercury within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg401

b:31.3
occ:1.00
SG A:CYS115 2.5 27.8 1.0
OD2 A:ASP105 2.7 24.9 1.0
OD1 A:ASP105 2.8 23.3 1.0
CG A:ASP105 3.2 26.3 1.0
CB A:CYS115 3.4 25.7 1.0
CA A:CYS115 3.6 25.7 1.0
CG2 A:THR50 3.7 15.1 1.0
CD A:LYS47 4.0 20.4 1.0
CB A:THR50 4.2 16.2 1.0
CG A:LYS47 4.3 18.5 1.0
NZ A:LYS47 4.5 22.9 1.0
C A:CYS115 4.5 25.5 1.0
O A:CYS115 4.6 26.0 1.0
CB A:LYS47 4.6 17.4 1.0
N A:CYS115 4.6 25.5 1.0
CB A:ASP105 4.7 27.6 1.0
CE A:LYS47 4.7 21.5 1.0
O A:VAL150 4.8 20.9 1.0
OG1 A:THR50 4.8 14.8 1.0
CD1 A:ILE54 4.8 23.9 1.0

Reference:

G.Nicola, A.Fedarovich, R.A.Nicholas, C.Davies. A Large Displacement of the Sxn Motif of CYS115-Modified Penicillin-Binding Protein 5 From Escherichia Coli. Biochem.J. V. 392 55 2005.
ISSN: ISSN 0264-6021
PubMed: 16038617
DOI: 10.1042/BJ20050449
Page generated: Sun Dec 13 19:05:16 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy