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Zinc in PDB 1rjp: Crystal Structure of D-Aminoacylase in Complex with 100MM CUCL2

Enzymatic activity of Crystal Structure of D-Aminoacylase in Complex with 100MM CUCL2

All present enzymatic activity of Crystal Structure of D-Aminoacylase in Complex with 100MM CUCL2:
3.5.1.81;

Protein crystallography data

The structure of Crystal Structure of D-Aminoacylase in Complex with 100MM CUCL2, PDB code: 1rjp 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) 28.10 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.343, 77.099, 135.891, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 21.6

Other elements in 1rjp:

The structure of Crystal Structure of D-Aminoacylase 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 Crystal Structure of D-Aminoacylase in Complex with 100MM CUCL2 (pdb code 1rjp). 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 D-Aminoacylase in Complex with 100MM CUCL2, PDB code: 1rjp:

Zinc binding site 1 out of 1 in 1rjp

Go back to Zinc Binding Sites List in 1rjp
Zinc binding site 1 out of 1 in the Crystal Structure of D-Aminoacylase 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 Crystal Structure of D-Aminoacylase in Complex with 100MM CUCL2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:11.5
occ:1.00
O A:ACT901 2.0 9.3 1.0
ND1 A:HIS220 2.1 7.3 1.0
NE2 A:HIS250 2.1 10.5 1.0
SG A:CYS96 2.3 9.4 1.0
OXT A:ACT901 2.6 10.9 1.0
C A:ACT901 2.6 9.9 1.0
CE1 A:HIS220 3.0 9.1 1.0
CG A:HIS220 3.0 6.6 1.0
CD2 A:HIS250 3.1 9.2 1.0
CE1 A:HIS250 3.1 11.2 1.0
CB A:CYS96 3.3 9.4 1.0
CU A:CU602 3.4 12.8 1.0
CB A:HIS220 3.4 6.6 1.0
NE2 A:HIS220 4.0 7.2 1.0
CH3 A:ACT902 4.1 9.9 1.0
CD2 A:HIS220 4.1 8.0 1.0
OH A:TYR192 4.1 12.9 1.0
CH3 A:ACT901 4.1 12.2 1.0
ND1 A:HIS250 4.2 10.6 1.0
CG A:HIS250 4.2 9.2 1.0
CE2 A:TYR192 4.4 11.1 1.0
NE2 A:HIS67 4.4 8.5 1.0
CA A:HIS220 4.5 8.0 1.0
CA A:CYS96 4.6 9.2 1.0
CE1 A:HIS67 4.6 6.1 1.0
CZ A:TYR192 4.7 12.6 1.0
OD2 A:ASP366 4.8 11.1 1.0
NE2 A:HIS69 4.9 9.2 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: Wed Dec 16 03:02:56 2020

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