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Zinc in PDB 5um3: Crystal Structure of the V122L Mutant of Human Ubr-Box Domain From UBR2

Enzymatic activity of Crystal Structure of the V122L Mutant of Human Ubr-Box Domain From UBR2

All present enzymatic activity of Crystal Structure of the V122L Mutant of Human Ubr-Box Domain From UBR2:
2.3.2.27;

Protein crystallography data

The structure of Crystal Structure of the V122L Mutant of Human Ubr-Box Domain From UBR2, PDB code: 5um3 was solved by J.Munoz Escobar, G.Kozlov, K.Gehring, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.62 / 1.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 29.177, 29.375, 66.052, 90.00, 90.00, 90.00
R / Rfree (%) 13.7 / 15.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the V122L Mutant of Human Ubr-Box Domain From UBR2 (pdb code 5um3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the V122L Mutant of Human Ubr-Box Domain From UBR2, PDB code: 5um3:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 5um3

Go back to Zinc Binding Sites List in 5um3
Zinc binding site 1 out of 3 in the Crystal Structure of the V122L Mutant of Human Ubr-Box Domain From UBR2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the V122L Mutant of Human Ubr-Box Domain From UBR2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:11.5
occ:1.00
SG A:CYS99 2.3 12.4 1.0
SG A:CYS149 2.3 11.8 1.0
SG A:CYS124 2.3 11.6 1.0
SG A:CYS127 2.4 11.3 1.0
HB2 A:CYS127 3.0 13.2 1.0
HB3 A:CYS149 3.1 13.6 1.0
CB A:CYS99 3.1 12.6 1.0
HB2 A:CYS99 3.1 15.1 1.0
CB A:CYS149 3.1 11.3 1.0
HB3 A:CYS99 3.1 15.1 1.0
HB2 A:CYS149 3.1 13.6 1.0
H A:CYS124 3.2 12.2 1.0
CB A:CYS127 3.3 11.0 1.0
HB3 A:CYS124 3.3 13.3 1.0
CB A:CYS124 3.5 11.1 1.0
HB3 A:CYS151 3.6 14.5 1.0
HE1 A:HIS166 3.8 17.4 1.0
HB2 A:CYS151 3.8 14.5 1.0
H A:CYS127 3.8 14.2 1.0
HB3 A:CYS127 3.8 13.2 1.0
HB3 A:ARG101 3.9 18.4 1.0
N A:CYS124 3.9 10.1 1.0
CB A:CYS151 4.2 12.1 1.0
HB2 A:ARG101 4.2 18.4 1.0
H A:ARG101 4.2 16.5 1.0
HB2 A:CYS124 4.2 13.3 1.0
CA A:CYS124 4.3 10.9 1.0
H A:CYS151 4.3 14.2 1.0
ZN A:ZN202 4.3 12.0 1.0
O A:HOH316 4.4 25.6 1.0
N A:CYS127 4.4 11.8 1.0
CE1 A:HIS166 4.4 14.5 1.0
CA A:CYS127 4.5 11.3 1.0
CB A:ARG101 4.5 15.3 1.0
CA A:CYS99 4.5 13.2 1.0
CA A:CYS149 4.6 11.9 1.0
HA A:LEU123 4.7 13.1 1.0
O A:HOH366 4.8 32.5 1.0
HB3 A:GLU126 4.8 24.0 1.0
HA A:CYS99 4.8 15.9 1.0
ND1 A:HIS166 4.9 14.0 1.0
HA A:CYS127 4.9 13.6 1.0
HD3 A:ARG101 4.9 21.0 1.0
HA A:CYS149 4.9 14.3 1.0
C A:CYS124 4.9 10.9 1.0
O A:CYS124 4.9 10.8 1.0

Zinc binding site 2 out of 3 in 5um3

Go back to Zinc Binding Sites List in 5um3
Zinc binding site 2 out of 3 in the Crystal Structure of the V122L Mutant of Human Ubr-Box Domain From UBR2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the V122L Mutant of Human Ubr-Box Domain From UBR2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn202

b:12.0
occ:1.00
ND1 A:HIS166 2.1 14.0 1.0
SG A:CYS151 2.3 14.4 1.0
SG A:CYS163 2.3 12.3 1.0
SG A:CYS127 2.4 11.3 1.0
HB2 A:HIS166 3.0 16.8 1.0
CE1 A:HIS166 3.0 14.5 1.0
HB3 A:CYS151 3.0 14.5 1.0
HB3 A:CYS127 3.0 13.2 1.0
HE1 A:HIS166 3.1 17.4 1.0
CG A:HIS166 3.1 13.8 1.0
CB A:CYS151 3.2 12.1 1.0
HB3 A:CYS163 3.2 14.8 1.0
CB A:CYS127 3.2 11.0 1.0
HB2 A:CYS99 3.3 15.1 1.0
H A:CYS163 3.3 15.4 1.0
HB2 A:CYS151 3.4 14.5 1.0
CB A:CYS163 3.4 12.3 1.0
HA A:CYS127 3.4 13.6 1.0
CB A:HIS166 3.6 14.0 1.0
H A:HIS166 3.8 17.0 1.0
HB3 A:LYS165 3.9 21.0 1.0
CA A:CYS127 3.9 11.3 1.0
HB2 A:CYS127 4.1 13.2 1.0
N A:CYS163 4.1 12.8 1.0
HB2 A:CYS163 4.1 14.8 1.0
NE2 A:HIS166 4.1 15.0 1.0
HB3 A:HIS166 4.2 16.8 1.0
CD2 A:HIS166 4.2 15.2 1.0
CB A:CYS99 4.3 12.6 1.0
CA A:CYS163 4.3 12.2 1.0
N A:HIS166 4.3 14.1 1.0
ZN A:ZN201 4.3 11.5 1.0
CA A:CYS151 4.6 11.6 1.0
CA A:HIS166 4.6 14.0 1.0
HB3 A:CYS99 4.6 15.1 1.0
H A:LYS165 4.6 17.1 1.0
HA A:TYR162 4.8 15.7 1.0
CB A:LYS165 4.8 17.5 1.0
HD3 A:LYS165 4.9 28.4 1.0
C A:CYS163 4.9 12.4 1.0
N A:CYS127 4.9 11.8 1.0
HE2 A:HIS166 4.9 18.0 1.0
HA A:CYS151 4.9 13.9 1.0
C A:CYS151 4.9 12.8 1.0
C A:CYS127 5.0 12.1 1.0
SG A:CYS99 5.0 12.4 1.0
O A:HOH352 5.0 16.2 1.0
H A:CYS99 5.0 16.1 1.0

Zinc binding site 3 out of 3 in 5um3

Go back to Zinc Binding Sites List in 5um3
Zinc binding site 3 out of 3 in the Crystal Structure of the V122L Mutant of Human Ubr-Box Domain From UBR2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the V122L Mutant of Human Ubr-Box Domain From UBR2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn203

b:13.3
occ:1.00
ND1 A:HIS136 2.0 14.4 1.0
ND1 A:HIS133 2.1 13.2 1.0
SG A:CYS112 2.3 13.4 1.0
SG A:CYS115 2.3 15.2 1.0
HB2 A:CYS115 2.8 19.3 1.0
CE1 A:HIS136 2.9 15.8 1.0
CE1 A:HIS133 2.9 12.8 1.0
HE1 A:HIS136 3.0 19.0 1.0
HE1 A:HIS133 3.0 15.3 1.0
CB A:CYS115 3.1 16.1 1.0
CG A:HIS136 3.1 14.8 1.0
HA A:HIS133 3.2 14.8 1.0
CG A:HIS133 3.2 12.8 1.0
HB3 A:HIS133 3.3 15.2 1.0
HB2 A:ASP114 3.3 20.6 1.0
HB2 A:HIS136 3.3 17.8 1.0
CB A:CYS112 3.4 12.7 1.0
HB3 A:CYS112 3.5 15.3 1.0
HB2 A:CYS112 3.5 15.3 1.0
HB3 A:HIS136 3.5 17.8 1.0
CB A:HIS136 3.6 14.8 1.0
CB A:HIS133 3.6 12.6 1.0
H A:CYS115 3.6 19.7 1.0
HB3 A:CYS115 3.8 19.3 1.0
HG13 A:ILE132 3.8 18.9 1.0
CA A:HIS133 3.8 12.4 1.0
N A:CYS115 3.9 16.4 1.0
NE2 A:HIS136 4.1 16.6 1.0
NE2 A:HIS133 4.1 12.8 1.0
CA A:CYS115 4.1 15.7 1.0
CD2 A:HIS136 4.2 15.8 1.0
CD2 A:HIS133 4.2 13.5 1.0
CB A:ASP114 4.3 17.1 1.0
H A:ASP114 4.5 19.3 1.0
HD11 A:ILE132 4.5 21.0 1.0
HB3 A:ASP114 4.5 20.6 1.0
N A:HIS133 4.5 12.4 1.0
HB2 A:HIS133 4.5 15.2 1.0
C A:ASP114 4.6 17.1 1.0
HA A:CYS115 4.6 18.8 1.0
CG1 A:ILE132 4.7 15.7 1.0
CA A:CYS112 4.7 12.8 1.0
H A:HIS133 4.8 14.9 1.0
HE2 A:HIS136 4.8 19.9 1.0
CA A:ASP114 4.8 16.3 1.0
HD12 A:ILE132 4.8 21.0 1.0
HB2 A:GLU159 4.8 19.4 1.0
HE2 A:HIS133 4.9 15.4 1.0
HA A:CYS112 4.9 15.4 1.0
CD1 A:ILE132 4.9 17.5 1.0
N A:ASP114 4.9 16.1 1.0

Reference:

J.Munoz-Escobar, E.Matta-Camacho, C.Cho, G.Kozlov, K.Gehring. Bound Waters Mediate Binding of Diverse Substrates to A Ubiquitin Ligase. Structure V. 25 719 2017.
ISSN: ISSN 1878-4186
PubMed: 28392261
DOI: 10.1016/J.STR.2017.03.004
Page generated: Mon Oct 28 11:17:24 2024

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