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Zinc in PDB 2g45: Co-Crystal Structure of Znf Ubp Domain From the Deubiquitinating Enzyme Isopeptidase T (Isot) in Complex with Ubiquitin

Enzymatic activity of Co-Crystal Structure of Znf Ubp Domain From the Deubiquitinating Enzyme Isopeptidase T (Isot) in Complex with Ubiquitin

All present enzymatic activity of Co-Crystal Structure of Znf Ubp Domain From the Deubiquitinating Enzyme Isopeptidase T (Isot) in Complex with Ubiquitin:
3.1.2.15;

Protein crystallography data

The structure of Co-Crystal Structure of Znf Ubp Domain From the Deubiquitinating Enzyme Isopeptidase T (Isot) in Complex with Ubiquitin, PDB code: 2g45 was solved by F.E.Reyes-Turcu, J.R.Horton, J.E.Mullally, A.Heroux, X.Cheng, K.D.Wilkinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.00 / 1.99
Space group P 64
Cell size a, b, c (Å), α, β, γ (°) 68.074, 68.074, 225.345, 90.00, 90.00, 120.00
R / Rfree (%) 22.9 / 26.8

Other elements in 2g45:

The structure of Co-Crystal Structure of Znf Ubp Domain From the Deubiquitinating Enzyme Isopeptidase T (Isot) in Complex with Ubiquitin also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Co-Crystal Structure of Znf Ubp Domain From the Deubiquitinating Enzyme Isopeptidase T (Isot) in Complex with Ubiquitin (pdb code 2g45). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Co-Crystal Structure of Znf Ubp Domain From the Deubiquitinating Enzyme Isopeptidase T (Isot) in Complex with Ubiquitin, PDB code: 2g45:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2g45

Go back to Zinc Binding Sites List in 2g45
Zinc binding site 1 out of 2 in the Co-Crystal Structure of Znf Ubp Domain From the Deubiquitinating Enzyme Isopeptidase T (Isot) in Complex with Ubiquitin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Co-Crystal Structure of Znf Ubp Domain From the Deubiquitinating Enzyme Isopeptidase T (Isot) in Complex with Ubiquitin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:30.2
occ:1.00
ND1 A:HIS232 2.0 28.0 1.0
SG A:CYS202 2.3 31.3 1.0
SG A:CYS219 2.3 28.9 1.0
SG A:CYS199 2.4 29.9 1.0
CE1 A:HIS232 2.9 29.2 1.0
CG A:HIS232 3.1 29.1 1.0
CB A:CYS199 3.2 29.2 1.0
CB A:CYS219 3.3 25.5 1.0
CB A:CYS202 3.4 32.6 1.0
CB A:HIS232 3.5 26.8 1.0
N A:CYS202 3.8 35.4 1.0
N A:CYS219 3.9 26.4 1.0
CB A:ASN230 4.0 28.1 1.0
NE2 A:HIS232 4.0 29.4 1.0
CA A:CYS202 4.1 35.0 1.0
CD2 A:HIS232 4.2 27.7 1.0
CA A:CYS219 4.2 24.9 1.0
C A:LYS201 4.2 37.3 1.0
CB A:LYS201 4.5 38.9 1.0
OD1 A:ASN230 4.6 28.9 1.0
CA A:LYS201 4.7 37.8 1.0
N A:HIS232 4.7 26.1 1.0
CA A:CYS199 4.7 31.1 1.0
N A:LYS201 4.7 37.5 1.0
CA A:HIS232 4.8 26.4 1.0
CG A:ASN230 4.8 27.2 1.0
C A:CYS202 4.8 35.1 1.0
O A:LYS201 4.8 39.1 1.0
CA A:ASN230 4.9 27.2 1.0
C A:ASN230 5.0 26.8 1.0
O A:ASN230 5.0 26.3 1.0

Zinc binding site 2 out of 2 in 2g45

Go back to Zinc Binding Sites List in 2g45
Zinc binding site 2 out of 2 in the Co-Crystal Structure of Znf Ubp Domain From the Deubiquitinating Enzyme Isopeptidase T (Isot) in Complex with Ubiquitin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Co-Crystal Structure of Znf Ubp Domain From the Deubiquitinating Enzyme Isopeptidase T (Isot) in Complex with Ubiquitin within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn402

b:29.9
occ:1.00
ND1 D:HIS232 2.0 28.2 1.0
SG D:CYS199 2.4 29.6 1.0
SG D:CYS219 2.4 30.2 1.0
SG D:CYS202 2.4 30.1 1.0
CE1 D:HIS232 2.9 29.3 1.0
CG D:HIS232 3.1 28.8 1.0
CB D:CYS199 3.2 29.1 1.0
CB D:CYS202 3.3 32.9 1.0
CB D:CYS219 3.4 26.7 1.0
CB D:HIS232 3.6 25.4 1.0
N D:CYS202 3.8 35.4 1.0
N D:CYS219 3.9 26.8 1.0
CB D:ASN230 4.0 27.1 1.0
NE2 D:HIS232 4.0 29.0 1.0
CA D:CYS202 4.1 35.1 1.0
CD2 D:HIS232 4.2 27.6 1.0
C D:LYS201 4.2 36.7 1.0
CA D:CYS219 4.3 25.3 1.0
CB D:LYS201 4.5 37.2 1.0
O D:LYS201 4.6 38.4 1.0
CA D:CYS199 4.7 31.9 1.0
CA D:LYS201 4.7 37.1 1.0
OD1 D:ASN230 4.7 28.7 1.0
N D:HIS232 4.7 26.0 1.0
N D:LYS201 4.7 37.2 1.0
CA D:HIS232 4.8 25.1 1.0
C D:CYS202 4.8 35.4 1.0
CG D:ASN230 4.9 26.0 1.0
CA D:ASN230 4.9 27.1 1.0
O D:ASN230 5.0 27.1 1.0
C D:ASN230 5.0 27.1 1.0

Reference:

F.E.Reyes-Turcu, J.R.Horton, J.E.Mullally, A.Heroux, X.Cheng, K.D.Wilkinson. The Ubiquitin Binding Domain Znf Ubp Recognizes the C-Terminal Diglycine Motif of Unanchored Ubiquitin. Cell(Cambridge,Mass.) V. 124 1197 2006.
ISSN: ISSN 0092-8674
PubMed: 16564012
DOI: 10.1016/J.CELL.2006.02.038
Page generated: Thu Oct 17 00:01:07 2024

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