Zinc in PDB 2zp9: The Nature of the Trap:Anti-Trap Complex
Protein crystallography data
The structure of The Nature of the Trap:Anti-Trap Complex, PDB code: 2zp9
was solved by
M.Watanabe,
J.G.Heddle,
S.Unzai,
S.Akashi,
S.Y.Park,
J.R.H.Tame,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
3.20
|
Space group
|
P 6
|
Cell size a, b, c (Å), α, β, γ (°)
|
197.134,
197.135,
56.658,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
30.3 /
32.5
|
Zinc Binding Sites:
The binding sites of Zinc atom in the The Nature of the Trap:Anti-Trap Complex
(pdb code 2zp9). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the
The Nature of the Trap:Anti-Trap Complex, PDB code: 2zp9:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
Zinc binding site 1 out
of 5 in 2zp9
Go back to
Zinc Binding Sites List in 2zp9
Zinc binding site 1 out
of 5 in the The Nature of the Trap:Anti-Trap Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of The Nature of the Trap:Anti-Trap Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn54
b:0.5
occ:1.00
|
SG
|
C:CYS12
|
1.8
|
85.8
|
1.0
|
SG
|
C:CYS26
|
2.3
|
86.1
|
1.0
|
SG
|
C:CYS15
|
2.7
|
86.0
|
1.0
|
SG
|
C:CYS29
|
2.8
|
85.1
|
1.0
|
CB
|
C:CYS12
|
3.0
|
85.6
|
1.0
|
CB
|
C:CYS29
|
3.3
|
85.6
|
1.0
|
N
|
C:CYS29
|
3.4
|
85.7
|
1.0
|
CB
|
C:CYS26
|
3.5
|
85.9
|
1.0
|
CB
|
C:ALA28
|
3.7
|
85.6
|
1.0
|
N
|
C:CYS15
|
3.7
|
85.6
|
1.0
|
CB
|
C:CYS15
|
3.7
|
85.6
|
1.0
|
CB
|
C:LYS14
|
4.0
|
85.7
|
1.0
|
CA
|
C:CYS29
|
4.0
|
85.7
|
1.0
|
C
|
C:ALA28
|
4.1
|
85.6
|
1.0
|
CA
|
C:ALA28
|
4.3
|
85.6
|
1.0
|
CA
|
C:CYS12
|
4.3
|
85.5
|
1.0
|
CA
|
C:CYS15
|
4.3
|
85.6
|
1.0
|
N
|
C:ALA28
|
4.4
|
85.6
|
1.0
|
C
|
C:LYS14
|
4.6
|
85.7
|
1.0
|
N
|
C:LYS14
|
4.6
|
85.7
|
1.0
|
CA
|
C:LYS14
|
4.6
|
85.7
|
1.0
|
C
|
C:CYS12
|
4.7
|
85.5
|
1.0
|
CA
|
C:CYS26
|
4.8
|
85.8
|
1.0
|
C
|
C:CYS26
|
4.9
|
85.8
|
1.0
|
CD1
|
C:ILE35
|
4.9
|
85.4
|
1.0
|
O
|
C:CYS12
|
4.9
|
85.5
|
1.0
|
CG
|
C:LYS14
|
5.0
|
85.9
|
1.0
|
O
|
C:CYS26
|
5.0
|
85.7
|
1.0
|
|
Zinc binding site 2 out
of 5 in 2zp9
Go back to
Zinc Binding Sites List in 2zp9
Zinc binding site 2 out
of 5 in the The Nature of the Trap:Anti-Trap Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of The Nature of the Trap:Anti-Trap Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn54
b:0.3
occ:1.00
|
SG
|
D:CYS12
|
2.0
|
85.3
|
1.0
|
SG
|
D:CYS15
|
2.1
|
85.2
|
1.0
|
SG
|
D:CYS26
|
2.3
|
85.7
|
1.0
|
CB
|
D:CYS12
|
2.8
|
85.4
|
1.0
|
SG
|
D:CYS29
|
2.8
|
85.8
|
1.0
|
CB
|
D:CYS15
|
3.2
|
85.5
|
1.0
|
CB
|
D:CYS26
|
3.3
|
85.8
|
1.0
|
N
|
D:CYS15
|
3.4
|
85.7
|
1.0
|
CB
|
D:CYS29
|
3.5
|
85.8
|
1.0
|
CA
|
D:CYS15
|
3.8
|
85.5
|
1.0
|
N
|
D:CYS29
|
4.0
|
85.7
|
1.0
|
CA
|
D:CYS12
|
4.2
|
85.5
|
1.0
|
CB
|
D:LYS14
|
4.3
|
85.6
|
1.0
|
CA
|
D:CYS29
|
4.4
|
85.7
|
1.0
|
CB
|
D:ALA28
|
4.5
|
85.6
|
1.0
|
C
|
D:LYS14
|
4.5
|
85.7
|
1.0
|
O
|
D:CYS12
|
4.5
|
85.5
|
1.0
|
C
|
D:CYS15
|
4.5
|
85.4
|
1.0
|
C
|
D:CYS12
|
4.6
|
85.5
|
1.0
|
O
|
D:CYS15
|
4.7
|
85.4
|
1.0
|
CA
|
D:LYS14
|
4.7
|
85.7
|
1.0
|
N
|
D:LYS14
|
4.8
|
85.7
|
1.0
|
CA
|
D:CYS26
|
4.8
|
85.8
|
1.0
|
C
|
D:ALA28
|
4.8
|
85.6
|
0.0
|
|
Zinc binding site 3 out
of 5 in 2zp9
Go back to
Zinc Binding Sites List in 2zp9
Zinc binding site 3 out
of 5 in the The Nature of the Trap:Anti-Trap Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of The Nature of the Trap:Anti-Trap Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn54
b:70.5
occ:1.00
|
SG
|
E:CYS12
|
2.2
|
85.3
|
1.0
|
SG
|
E:CYS26
|
2.3
|
85.3
|
1.0
|
SG
|
E:CYS29
|
2.3
|
84.4
|
1.0
|
SG
|
E:CYS15
|
2.5
|
85.5
|
1.0
|
CB
|
E:CYS29
|
2.6
|
85.4
|
1.0
|
CB
|
E:CYS12
|
3.1
|
85.5
|
1.0
|
N
|
E:CYS29
|
3.3
|
85.7
|
1.0
|
CB
|
E:CYS26
|
3.4
|
85.6
|
1.0
|
CA
|
E:CYS29
|
3.5
|
85.6
|
1.0
|
CB
|
E:CYS15
|
3.9
|
85.4
|
1.0
|
C
|
E:ALA28
|
4.2
|
85.6
|
1.0
|
N
|
E:CYS15
|
4.3
|
85.7
|
1.0
|
CB
|
E:ALA28
|
4.3
|
85.4
|
1.0
|
CA
|
E:GLY33
|
4.5
|
83.2
|
1.0
|
C
|
E:CYS29
|
4.5
|
85.7
|
1.0
|
CA
|
E:CYS12
|
4.6
|
85.5
|
1.0
|
CA
|
E:ALA28
|
4.7
|
85.5
|
1.0
|
N
|
E:GLY33
|
4.7
|
83.4
|
1.0
|
CA
|
E:CYS15
|
4.7
|
85.4
|
1.0
|
CA
|
E:CYS26
|
4.7
|
85.7
|
1.0
|
O
|
E:CYS26
|
4.7
|
85.7
|
1.0
|
CA
|
E:GLY19
|
4.8
|
77.3
|
1.0
|
N
|
E:ALA28
|
4.8
|
85.6
|
1.0
|
C
|
E:CYS26
|
4.8
|
85.7
|
1.0
|
N
|
E:SER30
|
4.9
|
85.8
|
1.0
|
CB
|
E:LYS14
|
5.0
|
85.8
|
1.0
|
|
Zinc binding site 4 out
of 5 in 2zp9
Go back to
Zinc Binding Sites List in 2zp9
Zinc binding site 4 out
of 5 in the The Nature of the Trap:Anti-Trap Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of The Nature of the Trap:Anti-Trap Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Zn54
b:0.7
occ:1.00
|
SG
|
I:CYS15
|
1.5
|
85.2
|
1.0
|
SG
|
I:CYS29
|
2.4
|
85.3
|
1.0
|
SG
|
I:CYS12
|
2.5
|
85.2
|
1.0
|
CB
|
I:CYS12
|
2.9
|
85.6
|
1.0
|
CB
|
I:CYS15
|
3.1
|
85.5
|
1.0
|
SG
|
I:CYS26
|
3.2
|
86.2
|
1.0
|
CB
|
I:CYS29
|
3.3
|
85.7
|
1.0
|
CB
|
I:CYS26
|
3.6
|
86.0
|
1.0
|
N
|
I:CYS15
|
3.9
|
85.7
|
1.0
|
CA
|
I:CYS15
|
3.9
|
85.5
|
1.0
|
CA
|
I:GLY33
|
4.2
|
85.9
|
1.0
|
C
|
I:CYS15
|
4.3
|
85.4
|
1.0
|
CA
|
I:CYS12
|
4.3
|
85.5
|
1.0
|
O
|
I:CYS15
|
4.3
|
85.5
|
1.0
|
C
|
I:GLY33
|
4.4
|
85.8
|
1.0
|
N
|
I:CYS29
|
4.4
|
85.7
|
1.0
|
N
|
I:GLY33
|
4.4
|
86.0
|
1.0
|
CA
|
I:CYS29
|
4.5
|
85.7
|
1.0
|
O
|
I:GLY33
|
4.5
|
85.6
|
1.0
|
O
|
I:CYS12
|
4.7
|
85.5
|
1.0
|
C
|
I:CYS12
|
4.8
|
85.5
|
1.0
|
N
|
I:VAL34
|
5.0
|
86.0
|
1.0
|
|
Zinc binding site 5 out
of 5 in 2zp9
Go back to
Zinc Binding Sites List in 2zp9
Zinc binding site 5 out
of 5 in the The Nature of the Trap:Anti-Trap Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of The Nature of the Trap:Anti-Trap Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Zn54
b:0.2
occ:1.00
|
SG
|
J:CYS29
|
2.1
|
85.0
|
1.0
|
SG
|
J:CYS15
|
2.2
|
86.0
|
1.0
|
SG
|
J:CYS12
|
2.4
|
85.5
|
1.0
|
SG
|
J:CYS26
|
2.5
|
85.8
|
1.0
|
CB
|
J:CYS26
|
3.1
|
85.8
|
1.0
|
CB
|
J:CYS29
|
3.1
|
85.8
|
1.0
|
CB
|
J:CYS12
|
3.5
|
85.5
|
1.0
|
CB
|
J:CYS15
|
3.5
|
85.5
|
1.0
|
N
|
J:CYS29
|
3.7
|
85.7
|
1.0
|
N
|
J:CYS15
|
3.9
|
85.7
|
1.0
|
CA
|
J:CYS29
|
4.0
|
85.7
|
1.0
|
CA
|
J:CYS15
|
4.3
|
85.6
|
1.0
|
CB
|
J:ALA28
|
4.5
|
85.5
|
1.0
|
CA
|
J:CYS26
|
4.5
|
85.8
|
1.0
|
C
|
J:ALA28
|
4.6
|
85.6
|
1.0
|
CA
|
J:GLY33
|
4.6
|
86.6
|
1.0
|
N
|
J:GLY33
|
4.7
|
86.3
|
1.0
|
O
|
J:CYS26
|
4.8
|
85.7
|
1.0
|
C
|
J:CYS26
|
4.8
|
85.7
|
1.0
|
CB
|
J:LYS14
|
4.8
|
85.7
|
1.0
|
CA
|
J:ALA28
|
4.9
|
85.6
|
1.0
|
C
|
J:CYS29
|
4.9
|
85.7
|
1.0
|
N
|
J:ALA28
|
4.9
|
85.6
|
1.0
|
CA
|
J:CYS12
|
4.9
|
85.5
|
1.0
|
C
|
J:CYS15
|
4.9
|
85.5
|
1.0
|
C
|
J:LYS14
|
5.0
|
85.7
|
1.0
|
|
Reference:
M.Watanabe,
J.G.Heddle,
K.Kikuchi,
S.Unzai,
S.Akashi,
S.Y.Park,
J.R.Tame.
The Nature of the Trap-Anti-Trap Complex. Proc.Natl.Acad.Sci.Usa V. 106 2176 2009.
ISSN: ISSN 0027-8424
PubMed: 19164760
DOI: 10.1073/PNAS.0801032106
Page generated: Thu Oct 24 10:52:17 2024
|