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Nickel in PDB 5a5e: Crystal Structure of Murd Ligase From Escherichia Coli

Enzymatic activity of Crystal Structure of Murd Ligase From Escherichia Coli

All present enzymatic activity of Crystal Structure of Murd Ligase From Escherichia Coli:
6.3.2.9;

Protein crystallography data

The structure of Crystal Structure of Murd Ligase From Escherichia Coli, PDB code: 5a5e was solved by R.Sink, M.Kotnik, A.Zega, H.Barreteau, S.Gobec, D.Blanot, A.Dessen, C.Contreras-Martel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.83 / 1.84
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.120, 70.433, 100.581, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 23.1

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of Murd Ligase From Escherichia Coli (pdb code 5a5e). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Crystal Structure of Murd Ligase From Escherichia Coli, PDB code: 5a5e:

Nickel binding site 1 out of 1 in 5a5e

Go back to Nickel Binding Sites List in 5a5e
Nickel binding site 1 out of 1 in the Crystal Structure of Murd Ligase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of Murd Ligase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni650

b:59.9
occ:1.00
ND1 A:HIS309 1.9 28.6 0.5
ND1 A:HIS309 1.9 27.9 0.5
CE1 A:HIS309 2.5 29.4 0.5
CE1 A:HIS309 2.8 27.8 0.5
CG A:HIS309 3.0 26.5 0.5
CG A:HIS309 3.0 26.3 0.5
CB A:HIS309 3.5 25.4 0.5
NE2 A:HIS309 3.6 29.6 0.5
CB A:HIS309 3.6 24.8 0.5
CD2 A:HIS309 3.8 26.9 0.5
CA A:HIS309 3.9 23.9 0.5
CA A:HIS309 3.9 24.1 0.5
NE2 A:HIS309 3.9 27.4 0.5
CD2 A:HIS309 4.0 25.7 0.5
O A:GLU308 4.4 21.8 1.0
N A:ASN310 4.8 23.9 1.0
C A:HIS309 4.9 23.5 1.0
N A:HIS309 5.0 22.6 1.0

Reference:

R.Sink, M.Kotnik, A.Zega, H.Barreteau, S.Gobec, D.Blanot, A.Dessen, C.Contreras-Martel. Crystallographic Study of Peptidoglycan Biosynthesis Enzyme Murd: Domain Movement Revisited. Plos One V. 11 52075 2016.
ISSN: ESSN 1932-6203
PubMed: 27031227
DOI: 10.1371/JOURNAL.PONE.0152075
Page generated: Thu Oct 10 06:12:27 2024

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