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Zinc in PDB 2zp8: The Nature of the Trap:Anti-Trap Complex

Protein crystallography data

The structure of The Nature of the Trap:Anti-Trap Complex, PDB code: 2zp8 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 H 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 201.134, 201.134, 133.168, 90.00, 90.00, 120.00
R / Rfree (%) 22.9 / 26.8

Zinc Binding Sites:

The binding sites of Zinc atom in the The Nature of the Trap:Anti-Trap Complex (pdb code 2zp8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the The Nature of the Trap:Anti-Trap Complex, PDB code: 2zp8:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 2zp8

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Zinc binding site 1 out of 6 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
E:Zn54

b:0.3
occ:1.00
SG E:CYS12 1.6 63.8 1.0
SG E:CYS26 2.9 64.3 1.0
CB E:CYS12 3.0 64.0 1.0
SG E:CYS15 3.0 64.4 1.0
CB E:LYS14 3.1 64.2 1.0
N E:CYS15 3.4 64.1 1.0
CB E:ALA28 3.5 64.3 1.0
N E:CYS29 3.5 64.1 1.0
CB E:CYS29 3.7 64.0 1.0
SG E:CYS29 3.8 63.3 1.0
N E:LYS14 3.8 64.1 1.0
CA E:LYS14 3.8 64.2 1.0
CB E:CYS15 4.0 64.0 1.0
C E:LYS14 4.0 64.2 1.0
CA E:CYS12 4.1 63.9 1.0
CG E:LYS14 4.1 64.4 1.0
CA E:CYS29 4.2 64.0 1.0
C E:CYS12 4.2 64.0 1.0
CA E:CYS15 4.3 64.0 1.0
C E:ALA28 4.3 64.1 1.0
CA E:ALA28 4.3 64.2 1.0
CD E:LYS14 4.4 64.3 1.0
O E:CYS12 4.4 64.1 1.0
CB E:CYS26 4.4 64.3 1.0
N E:ALA28 4.6 64.2 1.0
N E:PRO13 4.7 64.1 1.0
C E:PRO13 5.0 64.1 1.0

Zinc binding site 2 out of 6 in 2zp8

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Zinc binding site 2 out of 6 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
F:Zn54

b:78.2
occ:1.00
SG F:CYS15 2.1 62.7 1.0
SG F:CYS29 2.3 62.0 1.0
SG F:CYS26 2.3 64.4 1.0
SG F:CYS12 2.9 63.7 1.0
CB F:CYS29 2.9 63.6 1.0
CB F:CYS15 3.0 63.8 1.0
CB F:CYS26 3.1 64.3 1.0
CB F:CYS12 3.4 63.8 1.0
N F:CYS29 3.9 64.0 1.0
CA F:GLY33 4.0 64.2 1.0
CA F:CYS29 4.0 63.9 1.0
N F:CYS15 4.0 64.0 1.0
CA F:CYS15 4.1 63.9 1.0
N F:GLY33 4.2 64.3 1.0
CA F:GLY19 4.3 64.3 0.0
N F:GLY19 4.4 64.1 1.0
C F:GLY33 4.5 64.1 1.0
CA F:CYS26 4.6 64.3 1.0
O F:GLY33 4.7 64.0 1.0
CA F:CYS12 4.8 63.9 1.0
C F:CYS29 4.9 64.0 1.0
C F:GLY19 4.9 64.3 1.0
C F:CYS15 5.0 64.0 1.0

Zinc binding site 3 out of 6 in 2zp8

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Zinc binding site 3 out of 6 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
G:Zn54

b:71.9
occ:1.00
SG G:CYS29 2.4 63.2 1.0
SG G:CYS15 2.4 62.6 1.0
SG G:CYS26 2.4 63.2 1.0
SG G:CYS12 2.5 63.3 1.0
CB G:CYS29 3.0 63.8 1.0
CB G:CYS26 3.1 64.1 1.0
CB G:CYS15 3.4 63.6 1.0
CB G:CYS12 3.4 63.7 1.0
N G:CYS29 3.5 64.0 1.0
N G:CYS15 3.8 64.0 1.0
CA G:CYS29 3.8 64.0 1.0
CA G:CYS15 4.2 63.9 1.0
CB G:ALA28 4.5 64.0 1.0
CB G:LYS14 4.5 64.2 1.0
CA G:CYS26 4.5 64.2 1.0
C G:ALA28 4.6 64.1 1.0
CA G:GLY33 4.7 64.2 1.0
C G:CYS29 4.8 64.0 1.0
N G:GLY33 4.8 64.2 1.0
C G:LYS14 4.8 64.1 1.0
C G:CYS26 4.8 64.3 1.0
CA G:CYS12 4.8 63.8 1.0
N G:ALA28 4.8 64.2 1.0
CA G:ALA28 4.9 64.1 1.0
N G:SER30 4.9 64.0 1.0
CA G:GLY19 4.9 64.3 1.0

Zinc binding site 4 out of 6 in 2zp8

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Zinc binding site 4 out of 6 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
H:Zn54

b:0.8
occ:1.00
SG H:CYS12 1.6 64.0 1.0
SG H:CYS26 2.8 64.4 1.0
CB H:CYS12 2.9 64.1 1.0
N H:CYS29 3.2 64.1 1.0
CB H:CYS29 3.2 64.0 1.0
SG H:CYS15 3.2 64.2 1.0
SG H:CYS29 3.2 63.4 1.0
CB H:ALA28 3.6 64.2 1.0
CB H:LYS14 3.7 64.2 1.0
N H:CYS15 3.7 64.1 1.0
CA H:CYS29 3.8 64.0 1.0
CB H:CYS15 4.0 64.0 1.0
C H:ALA28 4.1 64.1 1.0
CB H:CYS26 4.1 64.3 1.0
CA H:ALA28 4.2 64.2 1.0
CA H:CYS12 4.2 63.9 1.0
N H:LYS14 4.3 64.1 1.0
CA H:LYS14 4.3 64.2 1.0
C H:LYS14 4.4 64.2 1.0
CA H:CYS15 4.5 64.0 1.0
C H:CYS12 4.5 64.0 1.0
N H:ALA28 4.5 64.2 1.0
O H:CYS12 4.6 64.1 1.0
CG H:LYS14 4.7 64.3 1.0
CD H:LYS14 4.9 64.4 1.0

Zinc binding site 5 out of 6 in 2zp8

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Zinc binding site 5 out of 6 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
I:Zn54

b:0.6
occ:1.00
SG I:CYS15 1.5 63.8 1.0
SG I:CYS29 2.7 64.2 1.0
CB I:CYS15 2.7 64.0 1.0
SG I:CYS26 2.7 64.3 1.0
SG I:CYS12 2.9 63.8 1.0
CB I:CYS12 3.1 63.8 1.0
CB I:CYS29 3.3 64.0 1.0
CB I:CYS26 3.5 64.3 1.0
N I:CYS15 3.6 64.1 1.0
CA I:CYS15 3.7 64.0 1.0
CA I:GLY33 4.0 64.2 1.0
N I:CYS29 4.3 64.0 1.0
N I:GLY19 4.3 64.2 1.0
N I:GLY33 4.3 64.2 1.0
CA I:CYS29 4.4 64.0 1.0
CA I:GLY19 4.4 64.3 0.0
C I:GLY33 4.4 64.1 1.0
O I:GLY33 4.5 64.0 1.0
C I:CYS15 4.5 64.0 1.0
CA I:CYS12 4.5 63.9 1.0
O I:CYS12 4.6 64.1 1.0
C I:LYS14 4.7 64.2 1.0
C I:CYS12 4.8 64.0 1.0
CB I:LYS14 5.0 64.2 1.0

Zinc binding site 6 out of 6 in 2zp8

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Zinc binding site 6 out of 6 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 6 of The Nature of the Trap:Anti-Trap Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn54

b:71.1
occ:1.00
SG J:CYS29 2.3 63.0 1.0
SG J:CYS12 2.3 63.5 1.0
SG J:CYS26 2.3 63.7 1.0
SG J:CYS15 2.5 62.6 1.0
CB J:CYS15 3.1 63.5 1.0
CB J:CYS29 3.2 63.8 1.0
CB J:CYS12 3.3 63.7 1.0
CB J:CYS26 3.3 64.1 1.0
N J:CYS15 3.6 64.0 1.0
N J:CYS29 3.7 64.0 1.0
CA J:CYS15 3.9 63.8 1.0
CA J:CYS29 4.0 64.0 1.0
CB J:LYS14 4.3 64.0 1.0
CB J:ALA28 4.5 63.9 1.0
C J:LYS14 4.6 64.1 1.0
CA J:CYS12 4.7 63.9 1.0
CA J:CYS26 4.7 64.2 1.0
CA J:GLY33 4.7 64.2 1.0
C J:ALA28 4.8 64.1 1.0
CA J:LYS14 4.8 64.1 1.0
O J:CYS12 4.9 64.0 1.0
N J:GLY33 4.9 64.1 1.0
C J:CYS15 4.9 63.9 1.0
C J:CYS12 5.0 64.0 1.0
N J:LYS14 5.0 64.1 1.0
CA J:GLY19 5.0 64.3 1.0
CA J:ALA28 5.0 64.1 1.0
N J:ALA28 5.0 64.2 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: Wed Dec 16 04:05:36 2020

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