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Zinc in PDB 4pqt: Insights Into the Mechanism of Deubiquitination By Jamm Deubiquitinases From Co-Crystal Structures of Enzyme with Substrate and Product

Protein crystallography data

The structure of Insights Into the Mechanism of Deubiquitination By Jamm Deubiquitinases From Co-Crystal Structures of Enzyme with Substrate and Product, PDB code: 4pqt was solved by R.K.Shrestha, J.A.Ronau, C.Das, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.11 / 2.05
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.413, 58.003, 56.189, 90.00, 108.97, 90.00
R / Rfree (%) 20.2 / 25.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Insights Into the Mechanism of Deubiquitination By Jamm Deubiquitinases From Co-Crystal Structures of Enzyme with Substrate and Product (pdb code 4pqt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Insights Into the Mechanism of Deubiquitination By Jamm Deubiquitinases From Co-Crystal Structures of Enzyme with Substrate and Product, PDB code: 4pqt:

Zinc binding site 1 out of 1 in 4pqt

Go back to Zinc Binding Sites List in 4pqt
Zinc binding site 1 out of 1 in the Insights Into the Mechanism of Deubiquitination By Jamm Deubiquitinases From Co-Crystal Structures of Enzyme with Substrate and Product


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Insights Into the Mechanism of Deubiquitination By Jamm Deubiquitinases From Co-Crystal Structures of Enzyme with Substrate and Product within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:29.9
occ:1.00
NE2 A:HIS406 1.8 28.0 1.0
NE2 A:HIS404 2.0 38.4 1.0
NE2 A:HIS356 2.1 31.2 1.0
SG A:CYS397 2.3 28.9 1.0
CE1 A:HIS406 2.7 25.6 1.0
CD2 A:HIS406 2.9 33.6 1.0
CE1 A:HIS404 3.0 39.2 1.0
CD2 A:HIS356 3.0 27.9 1.0
CD2 A:HIS404 3.1 36.6 1.0
CE1 A:HIS356 3.2 31.2 1.0
CB A:CYS397 3.4 29.2 1.0
ND1 A:HIS406 3.8 26.4 1.0
CG A:HIS406 4.0 26.6 1.0
ND1 A:HIS404 4.1 39.3 1.0
CG A:HIS404 4.2 40.2 1.0
CG A:HIS356 4.2 23.1 1.0
OG A:SER352 4.2 33.3 1.0
ND1 A:HIS356 4.3 27.0 1.0
CD1 A:ILE394 4.6 23.7 1.0
CB A:LYS399 4.7 37.3 1.0
CA A:CYS397 4.8 30.4 1.0
O A:LYS399 4.8 45.6 1.0
C A:CYS397 5.0 35.1 1.0

Reference:

R.K.Shrestha, J.A.Ronau, C.W.Davies, R.G.Guenette, E.R.Strieter, L.N.Paul, C.Das. Insights Into the Mechanism of Deubiquitination By Jamm Deubiquitinases From Cocrystal Structures of the Enzyme with the Substrate and Product. Biochemistry V. 53 3199 2014.
ISSN: ISSN 0006-2960
PubMed: 24787148
DOI: 10.1021/BI5003162
Page generated: Wed Dec 16 05:41:21 2020

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