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Zinc in PDB 5lda: Structure of Deubiquitinating Enzyme Homolog (Pyrococcus Furiosus JAMM1) in Complex with Ubiquitin-Like SAMP2.

Protein crystallography data

The structure of Structure of Deubiquitinating Enzyme Homolog (Pyrococcus Furiosus JAMM1) in Complex with Ubiquitin-Like SAMP2., PDB code: 5lda was solved by S.Cao, S.Engilberge, E.Girard, F.Gabel, B.Franzetti, J.A.Maupin-Furlow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.73 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.110, 37.233, 59.528, 90.00, 97.30, 90.00
R / Rfree (%) 17.4 / 21.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Deubiquitinating Enzyme Homolog (Pyrococcus Furiosus JAMM1) in Complex with Ubiquitin-Like SAMP2. (pdb code 5lda). 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 Structure of Deubiquitinating Enzyme Homolog (Pyrococcus Furiosus JAMM1) in Complex with Ubiquitin-Like SAMP2., PDB code: 5lda:

Zinc binding site 1 out of 1 in 5lda

Go back to Zinc Binding Sites List in 5lda
Zinc binding site 1 out of 1 in the Structure of Deubiquitinating Enzyme Homolog (Pyrococcus Furiosus JAMM1) in Complex with Ubiquitin-Like SAMP2.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Deubiquitinating Enzyme Homolog (Pyrococcus Furiosus JAMM1) in Complex with Ubiquitin-Like SAMP2. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:42.9
occ:0.80
NE2 A:HIS90 2.0 37.5 1.0
OXT B:GLY69 2.1 36.3 1.0
OD2 A:ASP101 2.1 34.7 1.0
NE2 A:HIS88 2.2 28.1 1.0
CG A:ASP101 2.8 47.1 1.0
OD1 A:ASP101 2.8 36.5 1.0
CD2 A:HIS90 2.9 38.3 1.0
C B:GLY69 2.9 37.9 1.0
CE1 A:HIS90 3.0 38.8 1.0
HD2 A:HIS90 3.1 45.9 1.0
CE1 A:HIS88 3.1 31.7 1.0
HE1 A:HIS88 3.2 38.0 1.0
CD2 A:HIS88 3.2 30.0 1.0
HE1 A:HIS90 3.2 46.5 1.0
H B:GLY69 3.4 40.8 1.0
O B:GLY69 3.4 37.4 1.0
HD2 A:HIS88 3.4 36.0 1.0
HD13 A:ILE114 3.5 31.6 1.0
O B:HOH703 3.5 94.5 1.0
H A:SER98 3.7 29.3 1.0
HG A:SER98 4.0 49.9 1.0
CA B:GLY69 4.0 43.3 1.0
OG A:SER98 4.0 41.6 1.0
N B:GLY69 4.0 34.0 1.0
HG21 A:ILE114 4.0 40.1 1.0
CG A:HIS90 4.1 25.9 1.0
ND1 A:HIS90 4.1 25.5 1.0
HA A:PRO97 4.1 31.2 1.0
HG23 A:ILE114 4.1 40.1 1.0
ND1 A:HIS88 4.2 32.4 1.0
CB A:ASP101 4.2 35.6 1.0
CD1 A:ILE114 4.3 26.4 1.0
CG A:HIS88 4.3 21.4 1.0
HB3 A:SER98 4.4 36.2 1.0
HD11 A:ILE114 4.4 31.6 1.0
HA2 B:GLY69 4.4 52.0 1.0
HE1 A:PHE62 4.5 35.0 1.0
HB2 A:ASP101 4.5 42.7 1.0
N A:SER98 4.5 24.4 1.0
HG12 A:ILE114 4.5 29.0 1.0
CG2 A:ILE114 4.5 33.4 1.0
HB3 A:ASP101 4.7 42.7 1.0
HA3 B:GLY69 4.7 52.0 1.0
CB A:SER98 4.7 30.2 1.0
O A:ILE96 4.8 31.8 1.0
CG1 A:ILE114 4.9 24.2 1.0
H A:ASP101 4.9 41.2 1.0
CA A:PRO97 5.0 26.0 1.0

Reference:

S.Cao, S.Engilberge, E.Girard, F.Gabel, B.Franzetti, J.A.Maupin-Furlow. Structural Insight Into Ubiquitin-Like Protein Recognition and Oligomeric States of Jamm/Mpn(+) Proteases. Structure V. 25 823 2017.
ISSN: ISSN 1878-4186
PubMed: 28479062
DOI: 10.1016/J.STR.2017.04.002
Page generated: Sun Oct 27 20:57:10 2024

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