Zinc in PDB 1yb0: Structure of Plyl
Protein crystallography data
The structure of Structure of Plyl, PDB code: 1yb0
was solved by
L.Y.Low,
C.Yang,
M.Perego,
A.Osterman,
R.C.Liddington,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.24 /
1.86
|
Space group
|
P 61
|
Cell size a, b, c (Å), α, β, γ (°)
|
163.181,
163.181,
37.292,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
20.6 /
24.2
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Plyl
(pdb code 1yb0). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Structure of Plyl, PDB code: 1yb0:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 1yb0
Go back to
Zinc Binding Sites List in 1yb0
Zinc binding site 1 out
of 3 in the Structure of Plyl
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structure of Plyl within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn160
b:23.0
occ:1.00
|
ND1
|
A:HIS29
|
2.2
|
19.5
|
1.0
|
ND1
|
A:HIS129
|
2.3
|
22.4
|
1.0
|
SG
|
A:CYS137
|
2.3
|
21.0
|
1.0
|
O4
|
A:PO4161
|
2.4
|
58.7
|
1.0
|
O2
|
A:PO4161
|
2.7
|
59.1
|
1.0
|
P
|
A:PO4161
|
3.0
|
63.0
|
1.0
|
CG
|
A:HIS29
|
3.1
|
21.3
|
1.0
|
CG
|
A:HIS129
|
3.1
|
21.3
|
1.0
|
CE1
|
A:HIS29
|
3.2
|
20.2
|
1.0
|
CB
|
A:CYS137
|
3.3
|
20.5
|
1.0
|
CB
|
A:HIS129
|
3.3
|
19.2
|
1.0
|
CE1
|
A:HIS129
|
3.3
|
24.4
|
1.0
|
CB
|
A:HIS29
|
3.4
|
19.6
|
1.0
|
O
|
A:HOH253
|
3.8
|
31.0
|
1.0
|
O3
|
A:PO4161
|
4.0
|
58.9
|
1.0
|
CA
|
A:HIS29
|
4.1
|
21.1
|
1.0
|
O1
|
A:PO4161
|
4.2
|
61.0
|
1.0
|
CD2
|
A:HIS29
|
4.3
|
20.3
|
1.0
|
NE2
|
A:HIS29
|
4.3
|
21.4
|
1.0
|
CD2
|
A:HIS129
|
4.3
|
23.0
|
1.0
|
NE2
|
A:HIS129
|
4.4
|
23.6
|
1.0
|
O
|
A:ALA74
|
4.4
|
23.6
|
1.0
|
OE2
|
A:GLU90
|
4.5
|
33.0
|
1.0
|
CA
|
A:CYS137
|
4.7
|
19.4
|
1.0
|
O
|
A:ASN30
|
4.7
|
22.1
|
1.0
|
CA
|
A:HIS129
|
4.8
|
19.1
|
1.0
|
N
|
A:ASN30
|
4.8
|
20.7
|
1.0
|
O
|
A:HOH163
|
5.0
|
20.4
|
1.0
|
|
Zinc binding site 2 out
of 3 in 1yb0
Go back to
Zinc Binding Sites List in 1yb0
Zinc binding site 2 out
of 3 in the Structure of Plyl
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structure of Plyl within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn160
b:22.7
occ:1.00
|
O2
|
B:PO41161
|
2.0
|
27.6
|
1.0
|
ND1
|
B:HIS29
|
2.1
|
22.6
|
1.0
|
ND1
|
B:HIS129
|
2.2
|
19.4
|
1.0
|
SG
|
B:CYS137
|
2.3
|
20.6
|
1.0
|
CG
|
B:HIS129
|
3.1
|
18.5
|
1.0
|
CE1
|
B:HIS29
|
3.1
|
22.4
|
1.0
|
CG
|
B:HIS29
|
3.1
|
22.8
|
1.0
|
P
|
B:PO41161
|
3.2
|
29.6
|
1.0
|
CE1
|
B:HIS129
|
3.2
|
21.2
|
1.0
|
CB
|
B:HIS129
|
3.3
|
18.0
|
1.0
|
CB
|
B:CYS137
|
3.3
|
19.5
|
1.0
|
CB
|
B:HIS29
|
3.4
|
21.4
|
1.0
|
O4
|
B:PO41161
|
3.5
|
28.4
|
1.0
|
O3
|
B:PO41161
|
3.8
|
27.2
|
1.0
|
O
|
B:ALA74
|
4.2
|
22.5
|
1.0
|
NE2
|
B:HIS29
|
4.2
|
23.4
|
1.0
|
CA
|
B:HIS29
|
4.2
|
20.5
|
1.0
|
CD2
|
B:HIS129
|
4.2
|
17.9
|
1.0
|
CD2
|
B:HIS29
|
4.2
|
24.1
|
1.0
|
NE2
|
B:HIS129
|
4.3
|
18.5
|
1.0
|
O1
|
B:PO41161
|
4.3
|
31.8
|
1.0
|
O
|
B:HOH1180
|
4.5
|
27.2
|
1.0
|
NZ
|
B:LYS135
|
4.6
|
29.0
|
1.0
|
CD
|
B:LYS135
|
4.7
|
23.5
|
1.0
|
OE2
|
B:GLU90
|
4.7
|
27.0
|
1.0
|
CE
|
B:LYS135
|
4.7
|
23.0
|
1.0
|
CA
|
B:CYS137
|
4.7
|
19.0
|
1.0
|
CA
|
B:HIS129
|
4.8
|
20.3
|
1.0
|
O
|
B:ASN30
|
4.9
|
21.9
|
1.0
|
N
|
B:ASN30
|
4.9
|
21.2
|
1.0
|
|
Zinc binding site 3 out
of 3 in 1yb0
Go back to
Zinc Binding Sites List in 1yb0
Zinc binding site 3 out
of 3 in the Structure of Plyl
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structure of Plyl within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn160
b:28.2
occ:1.00
|
ND1
|
C:HIS29
|
2.2
|
24.4
|
1.0
|
SG
|
C:CYS137
|
2.3
|
27.1
|
1.0
|
ND1
|
C:HIS129
|
2.3
|
23.9
|
1.0
|
O4
|
C:PO42161
|
2.6
|
67.2
|
1.0
|
O3
|
C:PO42161
|
2.7
|
65.4
|
1.0
|
P
|
C:PO42161
|
2.9
|
65.9
|
1.0
|
O1
|
C:PO42161
|
2.9
|
62.5
|
1.0
|
CG
|
C:HIS29
|
3.1
|
29.8
|
1.0
|
CG
|
C:HIS129
|
3.2
|
23.6
|
1.0
|
CB
|
C:CYS137
|
3.2
|
27.7
|
1.0
|
CB
|
C:HIS29
|
3.3
|
27.8
|
1.0
|
CE1
|
C:HIS29
|
3.3
|
27.0
|
1.0
|
CE1
|
C:HIS129
|
3.3
|
26.2
|
1.0
|
CB
|
C:HIS129
|
3.3
|
26.4
|
1.0
|
CA
|
C:HIS29
|
4.1
|
27.1
|
1.0
|
O
|
C:ALA74
|
4.1
|
27.0
|
1.0
|
CD2
|
C:HIS29
|
4.3
|
27.3
|
1.0
|
O2
|
C:PO42161
|
4.3
|
67.2
|
1.0
|
CD2
|
C:HIS129
|
4.3
|
25.8
|
1.0
|
OE2
|
C:GLU90
|
4.3
|
39.6
|
1.0
|
NE2
|
C:HIS29
|
4.3
|
26.5
|
1.0
|
NE2
|
C:HIS129
|
4.4
|
24.4
|
1.0
|
N
|
C:ASN30
|
4.6
|
30.7
|
1.0
|
CA
|
C:CYS137
|
4.7
|
25.8
|
1.0
|
O
|
C:ASN30
|
4.7
|
31.6
|
1.0
|
CA
|
C:HIS129
|
4.8
|
26.6
|
1.0
|
C
|
C:HIS29
|
5.0
|
32.1
|
1.0
|
C
|
C:CYS137
|
5.0
|
29.9
|
1.0
|
|
Reference:
L.Y.Low,
C.Yang,
M.Perego,
A.Osterman,
R.C.Liddington.
Structure and Lytic Activity of A Bacillus Anthracis Prophage Endolysin J.Biol.Chem. V. 280 35433 2005.
ISSN: ISSN 0021-9258
PubMed: 16103125
DOI: 10.1074/JBC.M502723200
Page generated: Wed Oct 16 20:49:12 2024
|