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Zinc in PDB 2lxp: uc(Nmr) Structure of Two Domains in Ubiquitin Ligase GP78, Ring and G2BR, Bound to Its Conjugating Enzyme UBE2G

Enzymatic activity of uc(Nmr) Structure of Two Domains in Ubiquitin Ligase GP78, Ring and G2BR, Bound to Its Conjugating Enzyme UBE2G

All present enzymatic activity of uc(Nmr) Structure of Two Domains in Ubiquitin Ligase GP78, Ring and G2BR, Bound to Its Conjugating Enzyme UBE2G:
6.3.2.19;

Zinc Binding Sites:

The binding sites of Zinc atom in the uc(Nmr) Structure of Two Domains in Ubiquitin Ligase GP78, Ring and G2BR, Bound to Its Conjugating Enzyme UBE2G (pdb code 2lxp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the uc(Nmr) Structure of Two Domains in Ubiquitin Ligase GP78, Ring and G2BR, Bound to Its Conjugating Enzyme UBE2G, PDB code: 2lxp:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2lxp

Go back to Zinc Binding Sites List in 2lxp
Zinc binding site 1 out of 2 in the uc(Nmr) Structure of Two Domains in Ubiquitin Ligase GP78, Ring and G2BR, Bound to Its Conjugating Enzyme UBE2G


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of uc(Nmr) Structure of Two Domains in Ubiquitin Ligase GP78, Ring and G2BR, Bound to Its Conjugating Enzyme UBE2G within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn900

b:0.4
occ:1.00
ND1 C:HIS361 1.8 0.4 1.0
SG C:CYS344 2.1 0.5 1.0
SG C:CYS364 2.2 0.4 1.0
SG C:CYS341 2.5 0.4 1.0
HB2 C:HIS361 2.6 0.4 1.0
CG C:HIS361 2.9 0.4 1.0
CE1 C:HIS361 2.9 0.5 1.0
HB2 C:CYS341 3.1 0.5 1.0
HE1 C:HIS361 3.2 0.6 1.0
CB C:HIS361 3.2 0.4 1.0
CB C:CYS341 3.3 0.4 1.0
HG3 C:MET348 3.4 0.9 1.0
HB3 C:CYS341 3.5 0.5 1.0
H C:HIS361 3.5 0.4 1.0
H C:CYS344 3.6 0.4 1.0
CB C:CYS344 3.7 0.5 1.0
CB C:CYS364 3.8 0.4 1.0
HB3 C:CYS344 3.8 0.5 1.0
HB3 C:HIS361 3.9 0.4 1.0
HB2 C:CYS364 3.9 0.4 1.0
CD2 C:HIS361 4.0 0.4 1.0
NE2 C:HIS361 4.0 0.5 1.0
HB3 C:CYS364 4.0 0.4 1.0
O C:TRP345 4.1 0.5 1.0
HB2 C:MET348 4.3 0.6 1.0
N C:HIS361 4.3 0.4 1.0
CA C:HIS361 4.3 0.4 1.0
N C:CYS344 4.4 0.4 1.0
HB2 C:CYS344 4.4 0.6 1.0
CG C:MET348 4.4 0.7 1.0
HB C:ILE343 4.4 0.3 1.0
CA C:CYS344 4.5 0.5 1.0
H C:TRP345 4.6 0.5 1.0
H C:CYS364 4.6 0.5 1.0
CA C:CYS341 4.7 0.5 1.0
N C:TRP345 4.8 0.5 1.0
HG2 C:MET348 4.8 0.9 1.0
C C:CYS344 4.8 0.5 1.0
HE2 C:HIS361 4.9 0.6 1.0
HA C:CYS341 4.9 0.5 1.0
CB C:MET348 4.9 0.5 1.0
HD2 C:HIS361 5.0 0.5 1.0

Zinc binding site 2 out of 2 in 2lxp

Go back to Zinc Binding Sites List in 2lxp
Zinc binding site 2 out of 2 in the uc(Nmr) Structure of Two Domains in Ubiquitin Ligase GP78, Ring and G2BR, Bound to Its Conjugating Enzyme UBE2G


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of uc(Nmr) Structure of Two Domains in Ubiquitin Ligase GP78, Ring and G2BR, Bound to Its Conjugating Enzyme UBE2G within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn901

b:0.8
occ:1.00
ND1 C:HIS358 1.8 0.8 1.0
SG C:CYS378 2.1 0.8 1.0
SG C:CYS375 2.2 0.7 1.0
SG C:CYS356 2.3 0.9 1.0
CE1 C:HIS358 2.7 1.0 1.0
HB2 C:CYS356 2.8 1.0 1.0
HE1 C:HIS358 2.8 1.1 1.0
CG C:HIS358 3.0 0.8 1.0
HB2 C:HIS358 3.0 0.7 1.0
HB3 C:CYS375 3.1 0.7 1.0
CB C:CYS356 3.1 0.9 1.0
CB C:CYS375 3.3 0.6 1.0
CB C:HIS358 3.5 0.7 1.0
HB2 C:CYS375 3.7 0.7 1.0
HB3 C:CYS356 3.7 1.0 1.0
CB C:CYS378 3.8 0.8 1.0
HE2 C:PHE360 3.8 0.8 1.0
NE2 C:HIS358 3.9 1.0 1.0
HB2 C:CYS378 4.0 0.8 1.0
CD2 C:HIS358 4.0 0.9 1.0
HB3 C:HIS358 4.1 0.7 1.0
HD22 C:LEU354 4.2 0.8 1.0
O C:CYS356 4.2 1.0 1.0
CA C:CYS356 4.3 1.0 1.0
C C:CYS356 4.4 1.0 1.0
HB3 C:CYS378 4.4 1.0 1.0
H C:THR377 4.5 0.5 1.0
HB C:THR377 4.5 0.7 1.0
C C:THR377 4.6 0.7 1.0
N C:CYS378 4.6 0.6 1.0
CA C:CYS375 4.6 0.6 1.0
HB2 C:LEU354 4.7 0.7 1.0
H C:CYS356 4.7 1.0 1.0
O C:THR377 4.7 1.2 1.0
HE2 C:HIS358 4.7 1.2 1.0
HB3 C:LEU354 4.7 0.8 1.0
CA C:HIS358 4.8 0.7 1.0
CA C:CYS378 4.8 0.8 1.0
N C:HIS358 4.8 0.8 1.0
CE2 C:PHE360 4.8 0.6 1.0
OG1 C:THR377 4.8 0.8 1.0
H C:HIS358 4.8 0.8 1.0
C C:CYS375 4.9 0.5 1.0
H C:CYS378 4.9 0.8 1.0
HD2 C:PRO376 5.0 0.5 1.0
N C:THR377 5.0 0.5 1.0

Reference:

R.Das, Y.H.Liang, J.Mariano, J.Li, T.Huang, A.King, S.G.Tarasov, A.M.Weissman, X.Ji, R.A.Byrd. Allosteric Regulation of E2:E3 Interactions Promote A Processive Ubiquitination Machine. Embo J. V. 32 2504 2013.
ISSN: ISSN 0261-4189
PubMed: 23942235
DOI: 10.1038/EMBOJ.2013.174
Page generated: Wed Dec 16 03:39:00 2020

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