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Copper 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

Copper Binding Sites:

The binding sites of Copper 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 Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of D-Aminoacylase in Complex with 100MM CUCL2, PDB code: 1rjp:

Copper binding site 1 out of 1 in 1rjp

Go back to Copper Binding Sites List in 1rjp
Copper 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 Copper with other atoms in the Cu 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:Cu602

b:12.8
occ:1.00
NE2 A:HIS69 2.0 9.2 1.0
NE2 A:HIS67 2.1 8.5 1.0
SG A:CYS96 2.3 9.4 1.0
OXT A:ACT901 2.6 10.9 1.0
CE1 A:HIS69 2.9 9.4 1.0
CE1 A:HIS67 2.9 6.1 1.0
CD2 A:HIS69 3.1 8.8 1.0
C A:ACT901 3.2 9.9 1.0
CD2 A:HIS67 3.2 6.0 1.0
ZN A:ZN601 3.4 11.5 1.0
OD1 A:ASP366 3.4 10.1 1.0
CB A:CYS96 3.5 9.4 1.0
O A:ACT901 3.7 9.3 1.0
CB A:ASN95 3.8 7.6 1.0
ND1 A:HIS69 4.0 8.8 1.0
CH3 A:ACT901 4.1 12.2 1.0
ND1 A:HIS67 4.1 8.4 1.0
CG A:HIS69 4.1 9.2 1.0
CG A:ASP366 4.2 9.6 1.0
CD2 A:HIS250 4.2 9.2 1.0
CG A:HIS67 4.3 9.0 1.0
C A:ASN95 4.3 8.0 1.0
N A:CYS96 4.3 8.0 1.0
NE2 A:HIS250 4.4 10.5 1.0
OD2 A:ASP366 4.4 11.1 1.0
O A:ASN95 4.5 6.3 1.0
CA A:CYS96 4.5 9.2 1.0
CA A:ASN95 4.7 8.8 1.0
CG A:ASN95 4.8 9.6 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: Thu Sep 3 16:16:00 2020
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