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Zinc in PDB 9c0f: Piggybat Transposase Protein-Dna Complex

Zinc Binding Sites:

The binding sites of Zinc atom in the Piggybat Transposase Protein-Dna Complex (pdb code 9c0f). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Piggybat Transposase Protein-Dna Complex, PDB code: 9c0f:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 9c0f

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Zinc binding site 1 out of 4 in the Piggybat Transposase Protein-Dna Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Piggybat Transposase Protein-Dna Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn601

b:89.0
occ:1.00
NE2 C:HIS567 1.9 71.8 1.0
ND1 C:HIS516 1.9 69.1 1.0
SG C:CYS550 2.2 65.7 1.0
SG C:CYS553 2.4 69.9 1.0
CE1 C:HIS516 2.8 69.1 1.0
CD2 C:HIS567 2.8 71.8 1.0
CE1 C:HIS567 3.0 71.8 1.0
CG C:HIS516 3.0 69.1 1.0
CB C:CYS550 3.5 65.7 1.0
CB C:HIS516 3.6 69.1 1.0
CB C:CYS553 3.9 69.9 1.0
NE2 C:HIS516 3.9 69.1 1.0
CG C:HIS567 4.0 71.8 1.0
CD2 C:HIS516 4.1 69.1 1.0
ND1 C:HIS567 4.1 71.8 1.0
CA C:HIS516 4.3 69.1 1.0
N C:CYS553 4.5 69.9 1.0
CA C:CYS550 4.8 65.7 1.0
CB C:PHE552 4.8 68.5 1.0
CA C:CYS553 4.9 69.9 1.0

Zinc binding site 2 out of 4 in 9c0f

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Zinc binding site 2 out of 4 in the Piggybat Transposase Protein-Dna Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Piggybat Transposase Protein-Dna Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn602

b:89.6
occ:1.00
ND1 C:HIS558 1.8 67.2 1.0
SG C:CYS562 2.2 70.3 1.0
SG C:CYS537 2.5 71.3 1.0
SG C:CYS534 2.7 67.0 1.0
CE1 C:HIS558 2.8 67.2 1.0
CG C:HIS558 3.0 67.2 1.0
CB C:HIS558 3.6 67.2 1.0
CB C:CYS534 3.6 67.0 1.0
CB C:CYS562 3.7 70.3 1.0
NE2 C:HIS558 3.9 67.2 1.0
CD2 C:HIS558 4.1 67.2 1.0
CB C:CYS537 4.1 71.3 1.0
N C:HIS558 4.4 67.2 1.0
OG C:SER544 4.5 69.8 1.0
CA C:HIS558 4.6 67.2 1.0
N C:CYS537 4.7 71.3 1.0
CA C:CYS562 4.9 70.3 1.0

Zinc binding site 3 out of 4 in 9c0f

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Zinc binding site 3 out of 4 in the Piggybat Transposase Protein-Dna Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Piggybat Transposase Protein-Dna Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn601

b:124.3
occ:1.00
ND1 D:HIS516 1.9 112.4 1.0
NE2 D:HIS567 1.9 111.2 1.0
CE1 D:HIS516 2.6 112.4 1.0
SG D:CYS550 2.6 104.2 1.0
SG D:CYS553 2.8 108.9 1.0
CD2 D:HIS567 2.8 111.2 1.0
CE1 D:HIS567 3.0 111.2 1.0
CG D:HIS516 3.0 112.4 1.0
NE2 D:HIS516 3.7 112.4 1.0
CB D:HIS516 3.8 112.4 1.0
CB D:CYS550 3.8 104.2 1.0
CB D:PHE552 3.9 109.8 1.0
CD2 D:HIS516 3.9 112.4 1.0
CG D:HIS567 4.0 111.2 1.0
ND1 D:HIS567 4.1 111.2 1.0
CB D:CYS553 4.1 108.9 1.0
N D:CYS553 4.2 108.9 1.0
CA D:HIS516 4.4 112.4 1.0
O D:CYS553 4.7 108.9 1.0
CG D:PHE552 4.7 109.8 1.0
CD2 D:PHE552 4.7 109.8 1.0
CA D:PHE552 4.8 109.8 1.0
CA D:CYS553 4.8 108.9 1.0
N D:PHE552 4.8 109.8 1.0
C D:PHE552 4.9 109.8 1.0

Zinc binding site 4 out of 4 in 9c0f

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Zinc binding site 4 out of 4 in the Piggybat Transposase Protein-Dna Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Piggybat Transposase Protein-Dna Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn602

b:140.7
occ:1.00
ND1 D:HIS558 2.2 107.3 1.0
SG D:CYS537 2.6 114.3 1.0
SG D:CYS562 2.7 105.2 1.0
CE1 D:HIS558 2.8 107.3 1.0
CG D:HIS558 3.1 107.3 1.0
SG D:CYS534 3.4 111.4 1.0
CB D:HIS558 3.6 107.3 1.0
NE2 D:HIS558 3.7 107.3 1.0
CD2 D:HIS558 3.8 107.3 1.0
CB D:CYS562 3.9 105.2 1.0
CB D:CYS534 4.0 111.4 1.0
CB D:CYS537 4.2 114.3 1.0
N D:HIS558 4.5 107.3 1.0
N D:CYS537 4.6 114.3 1.0
CA D:HIS558 4.6 107.3 1.0
CA D:CYS537 4.9 114.3 1.0
CB D:VAL536 5.0 112.8 1.0

Reference:

A.B.Hickman, L.Lannes, C.M.Furman, C.Hong, L.Franklin, R.Ghirlando, A.Ghosh, W.Luo, P.Konstantinidou, H.A.Lorenzi, A.Grove, A.D.Haase, M.H.Wilson, F.Dyda. Activity of the Mammalian Dna Transposon Piggybat From Myotis Lucifugus Is Restricted By Its Own Transposon Ends. Nat Commun V. 16 458 2025.
ISSN: ESSN 2041-1723
PubMed: 39774116
DOI: 10.1038/S41467-024-55784-9
Page generated: Sun Feb 9 09:12:17 2025

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