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Zinc in PDB 1rk5: The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2

Enzymatic activity of The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2

All present enzymatic activity of The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2:
3.5.1.81;

Protein crystallography data

The structure of The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2, PDB code: 1rk5 was solved by W.L.Lai, L.Y.Chou, C.Y.Ting, Y.C.Tsai, S.H.Liaw, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.40 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.016, 77.266, 135.982, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 20.4

Other elements in 1rk5:

The structure of The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2 also contains other interesting chemical elements:

Copper (Cu) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2 (pdb code 1rk5). 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 D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2, PDB code: 1rk5:

Zinc binding site 1 out of 1 in 1rk5

Go back to Zinc Binding Sites List in 1rk5
Zinc binding site 1 out of 1 in the The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:10.5
occ:1.00
O A:ACT901 2.0 16.5 1.0
ND1 A:HIS220 2.1 7.9 1.0
NE2 A:HIS250 2.2 10.8 1.0
SG A:CYS96 2.3 8.0 1.0
C A:ACT901 2.6 17.7 1.0
OXT A:ACT901 2.7 15.0 1.0
CE1 A:HIS220 2.9 7.6 1.0
CG A:HIS220 3.1 7.8 1.0
CD2 A:HIS250 3.2 10.3 1.0
CE1 A:HIS250 3.2 10.7 1.0
CU A:CU602 3.2 10.2 1.0
CB A:CYS96 3.4 9.0 1.0
CB A:HIS220 3.5 8.7 1.0
NE2 A:HIS220 4.0 9.2 1.0
OH A:TYR192 4.0 10.5 1.0
CH3 A:ACT901 4.1 17.3 1.0
CD2 A:HIS220 4.1 9.3 1.0
NE2 A:HIS67 4.3 7.3 1.0
CH3 A:ACT902 4.3 11.5 1.0
ND1 A:HIS250 4.3 8.9 1.0
CG A:HIS250 4.3 10.1 1.0
CE2 A:TYR192 4.4 11.8 1.0
CE1 A:HIS67 4.6 7.7 1.0
CA A:HIS220 4.6 8.4 1.0
CA A:CYS96 4.6 8.6 1.0
CZ A:TYR192 4.7 12.4 1.0
NE2 A:HIS69 4.8 14.4 1.0

Reference:

W.L.Lai, L.Y.Chou, C.Y.Ting, R.Kirby, Y.C.Tsai, A.H.Wang, S.H.Liaw. The Functional Role of the Binuclear Metal Center in D-Aminoacylase: One-Metal Activation and Second-Metal Attenuation. J.Biol.Chem. V. 279 13962 2004.
ISSN: ISSN 0021-9258
PubMed: 14736882
DOI: 10.1074/JBC.M308849200
Page generated: Mon Jan 25 16:12:43 2021

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