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Zinc in PDB 3nh8: Crystal Structure of Murine Aminoacylase 3 in Complex with N-Acetyl-S- 1,2-Dichlorovinyl-L-Cysteine

Protein crystallography data

The structure of Crystal Structure of Murine Aminoacylase 3 in Complex with N-Acetyl-S- 1,2-Dichlorovinyl-L-Cysteine, PDB code: 3nh8 was solved by J.M.Hsieh, K.Tsirulnikov, M.R.Sawaya, N.Magilnick, N.Abuladze, I.Kurtz, J.Abramson, A.Pushkin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.13 / 2.80
Space group P 62
Cell size a, b, c (Å), α, β, γ (°) 93.407, 93.407, 97.637, 90.00, 90.00, 120.00
R / Rfree (%) 17.5 / 22.4

Other elements in 3nh8:

The structure of Crystal Structure of Murine Aminoacylase 3 in Complex with N-Acetyl-S- 1,2-Dichlorovinyl-L-Cysteine also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Murine Aminoacylase 3 in Complex with N-Acetyl-S- 1,2-Dichlorovinyl-L-Cysteine (pdb code 3nh8). 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 Crystal Structure of Murine Aminoacylase 3 in Complex with N-Acetyl-S- 1,2-Dichlorovinyl-L-Cysteine, PDB code: 3nh8:

Zinc binding site 1 out of 1 in 3nh8

Go back to Zinc Binding Sites List in 3nh8
Zinc binding site 1 out of 1 in the Crystal Structure of Murine Aminoacylase 3 in Complex with N-Acetyl-S- 1,2-Dichlorovinyl-L-Cysteine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Murine Aminoacylase 3 in Complex with N-Acetyl-S- 1,2-Dichlorovinyl-L-Cysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn319

b:68.7
occ:1.00
O7 A:DC2322 2.3 42.9 1.0
OE1 A:GLU24 2.3 37.4 1.0
ND1 A:HIS116 2.4 36.1 1.0
ND1 A:HIS21 2.5 37.1 1.0
OE2 A:GLU24 2.5 37.9 1.0
CD A:GLU24 2.7 35.5 1.0
CE1 A:HIS21 3.0 40.7 1.0
CG A:HIS116 3.2 33.5 1.0
C6 A:DC2322 3.2 39.2 1.0
CE1 A:HIS116 3.3 37.5 1.0
C4 A:DC2322 3.3 45.4 1.0
N A:DC2322 3.3 31.9 1.0
CB A:HIS116 3.4 31.6 1.0
CG A:HIS21 3.8 36.9 1.0
O A:ASN117 4.0 36.4 1.0
C2 A:DC2322 4.1 52.9 1.0
CA A:HIS116 4.2 30.7 1.0
CG A:GLU24 4.2 32.9 1.0
CD2 A:HIS116 4.2 35.8 1.0
NE2 A:HIS116 4.3 37.7 1.0
NH1 A:ARG63 4.3 42.2 1.0
NE2 A:HIS21 4.3 37.2 1.0
O1 A:DC2322 4.4 52.4 1.0
CB A:HIS21 4.4 33.3 1.0
N A:ASN117 4.5 28.4 1.0
C8 A:DC2322 4.5 45.0 1.0
C9 A:DC2322 4.5 54.8 1.0
CD2 A:HIS21 4.7 36.1 1.0
OXT A:DC2322 4.8 53.7 1.0
C A:HIS116 4.8 29.8 1.0
NH2 A:ARG63 4.8 42.5 1.0
CB A:GLU24 4.9 29.3 1.0
CZ A:ARG63 4.9 40.2 1.0

Reference:

J.M.Hsieh, K.Tsirulnikov, M.R.Sawaya, N.Magilnick, N.Abuladze, I.Kurtz, J.Abramson, A.Pushkin. Structures of Aminoacylase 3 in Complex with Acetylated Substrates. Proc.Natl.Acad.Sci.Usa V. 107 17962 2010.
ISSN: ISSN 0027-8424
PubMed: 20921362
DOI: 10.1073/PNAS.1006687107
Page generated: Wed Dec 16 04:38:02 2020

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