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Zinc in PDB 1q7l: Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I

Enzymatic activity of Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I

All present enzymatic activity of Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I:
3.5.1.14;

Protein crystallography data

The structure of Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I, PDB code: 1q7l was solved by H.A.Lindner, V.V.Lunin, A.Alary, R.Hecker, M.Cygler, R.Menard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.71 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.528, 67.249, 146.479, 90.00, 90.00, 90.00
R / Rfree (%) 13.3 / 17.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I (pdb code 1q7l). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I, PDB code: 1q7l:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1q7l

Go back to Zinc Binding Sites List in 1q7l
Zinc binding site 1 out of 4 in the Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1002

b:9.4
occ:1.00
O C:HOH701 1.9 7.3 0.5
OE1 A:GLU175 2.0 9.5 1.0
OD1 A:ASP113 2.0 8.7 1.0
NE2 A:HIS80 2.0 8.3 1.0
O C:GLY901 2.0 12.8 0.5
OE2 A:GLU175 2.5 9.0 1.0
CD A:GLU175 2.6 8.2 1.0
CE1 A:HIS80 3.0 9.0 1.0
CG A:ASP113 3.0 9.7 1.0
CD2 A:HIS80 3.0 8.2 1.0
C C:GLY901 3.1 15.0 0.5
OD2 A:ASP113 3.3 10.2 1.0
ZN A:ZN1001 3.4 12.0 1.0
OE1 A:GLU147 3.5 12.6 1.0
OE2 A:GLU148 3.6 11.5 1.0
CA C:GLY901 3.9 16.5 0.5
OXT C:GLY901 4.0 18.4 0.5
CG A:GLU175 4.1 8.4 1.0
CD A:GLU147 4.1 11.0 1.0
ND1 A:HIS80 4.1 8.6 1.0
CG A:HIS80 4.2 8.2 1.0
O A:HOH1036 4.2 11.3 1.0
CB A:MET114 4.3 8.4 1.0
CB A:ASP113 4.3 9.2 1.0
O C:HOH703 4.3 17.9 0.5
CD A:GLU148 4.3 11.5 1.0
CG A:MET114 4.4 8.3 1.0
OE2 A:GLU147 4.4 16.1 1.0
SD A:MET114 4.5 8.5 1.0
C A:ASP113 4.6 8.6 1.0
CA A:ASP113 4.6 8.5 1.0
OE1 A:GLU148 4.6 10.5 1.0
CB A:GLU175 4.7 8.6 1.0
N A:MET114 4.8 8.0 1.0
O A:ASP113 4.9 9.1 1.0
N C:GLY901 4.9 19.3 0.5
O A:HOH1009 4.9 9.8 1.0

Zinc binding site 2 out of 4 in 1q7l

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Zinc binding site 2 out of 4 in the Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:12.0
occ:1.00
OE2 A:GLU148 2.0 11.5 1.0
OD2 A:ASP113 2.0 10.2 1.0
NE2 B:HIS373 2.0 10.4 1.0
O C:GLY901 2.1 12.8 0.5
O C:HOH701 2.1 7.3 0.5
O C:HOH703 2.2 17.9 0.5
OE1 A:GLU148 2.4 10.5 1.0
OXT C:GLY901 2.5 18.4 0.5
CD A:GLU148 2.5 11.5 1.0
C C:GLY901 2.8 15.0 0.5
CG A:ASP113 3.0 9.7 1.0
CE1 B:HIS373 3.0 12.0 1.0
CD2 B:HIS373 3.1 10.0 1.0
OD1 A:ASP113 3.3 8.7 1.0
ZN A:ZN1002 3.4 9.4 1.0
O A:HOH1027 3.9 10.3 1.0
CG A:GLU148 4.0 10.1 1.0
ND1 B:HIS373 4.1 12.8 1.0
OE1 A:GLU147 4.1 12.6 1.0
CG B:HIS373 4.2 9.4 1.0
CA C:GLY901 4.3 16.5 0.5
CB A:ASP113 4.3 9.2 1.0
CG1 A:VAL84 4.4 9.0 1.0
NE2 A:HIS80 4.5 8.3 1.0
O C:HOH1564 4.6 32.7 1.0
CE1 A:HIS80 4.6 9.0 1.0
CD1 B:LEU372 4.6 16.2 1.0
OE1 A:GLU175 4.8 9.5 1.0
O A:HOH1094 4.9 34.5 1.0

Zinc binding site 3 out of 4 in 1q7l

Go back to Zinc Binding Sites List in 1q7l
Zinc binding site 3 out of 4 in the Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1012

b:9.6
occ:1.00
O C:HOH702 1.9 9.9 0.5
OE1 C:GLU175 2.0 10.1 1.0
OD1 C:ASP113 2.0 9.0 1.0
O C:GLY902 2.0 12.4 0.5
NE2 C:HIS80 2.0 9.1 1.0
OE2 C:GLU175 2.5 9.7 1.0
CD C:GLU175 2.6 8.0 1.0
CE1 C:HIS80 2.9 9.4 1.0
CG C:ASP113 3.0 8.5 1.0
C C:GLY902 3.1 13.1 0.5
CD2 C:HIS80 3.1 8.5 1.0
OD2 C:ASP113 3.4 9.5 1.0
ZN C:ZN1011 3.4 11.9 1.0
OE1 C:GLU147 3.6 12.1 1.0
OE2 C:GLU148 3.6 11.4 1.0
CA C:GLY902 3.9 17.0 0.5
OXT C:GLY902 3.9 15.1 0.5
CD C:GLU147 4.1 12.4 1.0
ND1 C:HIS80 4.1 8.8 1.0
CG C:GLU175 4.1 9.7 1.0
CG C:HIS80 4.2 8.5 1.0
CB C:MET114 4.2 8.2 1.0
O C:HOH1087 4.2 13.2 1.0
OE2 C:GLU147 4.3 18.1 1.0
CB C:ASP113 4.3 8.7 1.0
CG C:MET114 4.3 8.2 1.0
CD C:GLU148 4.4 9.8 1.0
SD C:MET114 4.5 9.0 1.0
O C:HOH704 4.5 14.9 0.5
C C:ASP113 4.5 8.6 1.0
OE1 C:GLU148 4.6 11.9 1.0
CA C:ASP113 4.6 7.9 1.0
N C:GLY902 4.7 19.3 0.5
CB C:GLU175 4.7 9.6 1.0
N C:MET114 4.8 7.8 1.0
O C:ASP113 4.9 8.2 1.0
O C:HOH1061 5.0 11.5 1.0

Zinc binding site 4 out of 4 in 1q7l

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Zinc binding site 4 out of 4 in the Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Zn-Binding Domain of the T347G Mutant of Human Aminoacylase- I within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1011

b:11.9
occ:1.00
OE2 C:GLU148 2.0 11.4 1.0
OXT C:GLY902 2.0 15.1 0.5
NE2 D:HIS373 2.0 9.6 1.0
OD2 C:ASP113 2.0 9.5 1.0
O C:GLY902 2.0 12.4 0.5
OE1 C:GLU148 2.2 11.9 1.0
O C:HOH702 2.4 9.9 0.5
O C:HOH704 2.5 14.9 0.5
CD C:GLU148 2.6 9.8 1.0
C C:GLY902 2.6 13.1 0.5
CE1 D:HIS373 3.0 12.3 1.0
CG C:ASP113 3.0 8.5 1.0
CD2 D:HIS373 3.0 9.2 1.0
OD1 C:ASP113 3.4 9.0 1.0
ZN C:ZN1012 3.4 9.6 1.0
O C:HOH1004 4.0 9.2 1.0
CA C:GLY902 4.1 17.0 0.5
CG C:GLU148 4.1 9.7 1.0
ND1 D:HIS373 4.1 11.5 1.0
CG D:HIS373 4.2 9.5 1.0
OE1 C:GLU147 4.2 12.1 1.0
CB C:ASP113 4.3 8.7 1.0
CG1 C:VAL84 4.5 9.9 1.0
O C:HOH1318 4.6 27.9 1.0
NE2 C:HIS80 4.6 9.1 1.0
CD1 D:LEU372 4.6 18.7 1.0
CE1 C:HIS80 4.6 9.4 1.0
N C:GLY902 4.7 19.3 0.5
OE1 C:GLU175 4.9 10.1 1.0
O C:HOH1305 4.9 28.6 1.0

Reference:

H.A.Lindner, V.V.Lunin, A.Alary, R.Hecker, M.Cygler, R.Menard. Essential Roles of Zinc Ligation and Enzyme Dimerization For Catalysis in the Aminoacylase-1/M20 Family. J.Biol.Chem. V. 278 44496 2003.
ISSN: ISSN 0021-9258
PubMed: 12933810
DOI: 10.1074/JBC.M304233200
Page generated: Wed Dec 16 03:01:42 2020

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