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Zinc in PDB 3ne8: The Crystal Structure of A Domain From N-Acetylmuramoyl-L-Alanine Amidase of Bartonella Henselae Str. Houston-1

Protein crystallography data

The structure of The Crystal Structure of A Domain From N-Acetylmuramoyl-L-Alanine Amidase of Bartonella Henselae Str. Houston-1, PDB code: 3ne8 was solved by K.Tan, E.Rakowski, K.Buck, A.Joachimiak, Midwest Center For Structuralgenomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.25 / 1.24
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 71.185, 53.511, 58.495, 90.00, 90.46, 90.00
R / Rfree (%) 16.1 / 17.4

Zinc Binding Sites:

The binding sites of Zinc atom in the The Crystal Structure of A Domain From N-Acetylmuramoyl-L-Alanine Amidase of Bartonella Henselae Str. Houston-1 (pdb code 3ne8). 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 The Crystal Structure of A Domain From N-Acetylmuramoyl-L-Alanine Amidase of Bartonella Henselae Str. Houston-1, PDB code: 3ne8:

Zinc binding site 1 out of 1 in 3ne8

Go back to Zinc Binding Sites List in 3ne8
Zinc binding site 1 out of 1 in the The Crystal Structure of A Domain From N-Acetylmuramoyl-L-Alanine Amidase of Bartonella Henselae Str. Houston-1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of A Domain From N-Acetylmuramoyl-L-Alanine Amidase of Bartonella Henselae Str. Houston-1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:9.0
occ:0.71
OD1 A:ASP259 2.1 16.4 1.0
NE2 A:HIS188 2.2 10.3 1.0
ND1 A:HIS257 2.2 9.3 1.0
OE2 A:GLU290 2.2 12.3 1.0
OE2 A:GLU203 2.2 10.0 1.0
OD2 A:ASP259 2.6 14.8 1.0
CG A:ASP259 2.7 15.3 1.0
CD A:GLU290 3.0 15.8 1.0
CD A:GLU203 3.1 10.5 1.0
CE1 A:HIS257 3.1 10.5 1.0
CE1 A:HIS188 3.1 10.6 1.0
CD2 A:HIS188 3.2 9.6 1.0
CG A:HIS257 3.2 8.3 1.0
OE1 A:GLU203 3.3 11.4 1.0
OE1 A:GLU290 3.5 19.7 1.0
CB A:HIS257 3.6 9.0 1.0
O A:HOH93 3.7 19.3 1.0
CB A:ASP259 4.1 13.3 1.0
CG A:GLU290 4.2 15.7 1.0
NE2 A:HIS257 4.2 10.3 1.0
ND1 A:HIS188 4.3 10.5 1.0
CG A:HIS188 4.3 9.7 1.0
CD2 A:HIS257 4.3 9.8 1.0
O A:HOH22 4.3 10.9 1.0
CA A:HIS257 4.4 8.6 1.0
CG A:GLU203 4.4 9.7 1.0
N A:ALA258 4.5 9.2 1.0
CA A:ASP259 4.6 11.9 1.0
N A:ASP259 4.7 11.0 1.0
OE2 A:GLU365 4.9 13.9 1.0
C A:HIS257 5.0 8.9 1.0

Reference:

D.C.Yang, K.Tan, A.Joachimiak, T.G.Bernhardt. A Conformational Switch Controls Cell Wall-Remodelling Enzymes Required For Bacterial Cell Division. Mol.Microbiol. V. 85 768 2012.
ISSN: ISSN 0950-382X
PubMed: 22715947
DOI: 10.1111/J.1365-2958.2012.08138.X
Page generated: Sat Oct 26 10:11:58 2024

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