Zinc in PDB 9egw: Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled)
Enzymatic activity of Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled)
All present enzymatic activity of Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled):
2.3.2.31;
Protein crystallography data
The structure of Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled), PDB code: 9egw
was solved by
X.S.Wang,
B.C.Lechtenberg,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.86 /
1.78
|
Space group
|
I 41 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
96.063,
96.063,
187.434,
90,
90,
90
|
R / Rfree (%)
|
16.5 /
18.2
|
Other elements in 9egw:
The structure of Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled) also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled)
(pdb code 9egw). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the
Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled), PDB code: 9egw:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 9egw
Go back to
Zinc Binding Sites List in 9egw
Zinc binding site 1 out
of 6 in the Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn601
b:25.0
occ:1.00
|
SG
|
A:CYS450
|
2.3
|
25.6
|
1.0
|
SG
|
A:CYS468
|
2.3
|
25.8
|
1.0
|
SG
|
A:CYS465
|
2.4
|
25.9
|
1.0
|
SG
|
A:CYS447
|
2.4
|
23.7
|
1.0
|
HB3
|
A:CYS465
|
3.0
|
30.3
|
1.0
|
H
|
A:CYS450
|
3.1
|
27.3
|
1.0
|
CB
|
A:CYS465
|
3.1
|
25.2
|
1.0
|
HB3
|
A:CYS450
|
3.1
|
31.8
|
1.0
|
HB3
|
A:CYS447
|
3.2
|
29.5
|
1.0
|
HB2
|
A:CYS465
|
3.2
|
30.3
|
1.0
|
CB
|
A:CYS447
|
3.2
|
24.6
|
1.0
|
HB2
|
A:CYS447
|
3.3
|
29.5
|
1.0
|
H
|
A:CYS468
|
3.3
|
31.7
|
1.0
|
CB
|
A:CYS450
|
3.3
|
26.5
|
1.0
|
HB3
|
A:CYS468
|
3.4
|
30.8
|
1.0
|
HB
|
A:VAL467
|
3.5
|
36.3
|
1.0
|
CB
|
A:CYS468
|
3.5
|
25.6
|
1.0
|
N
|
A:CYS450
|
3.8
|
22.8
|
1.0
|
HB3
|
A:GLN449
|
3.8
|
26.1
|
1.0
|
N
|
A:CYS468
|
3.9
|
26.4
|
1.0
|
HG22
|
A:ILE452
|
4.0
|
37.9
|
1.0
|
CA
|
A:CYS450
|
4.1
|
23.0
|
1.0
|
HB2
|
A:CYS450
|
4.1
|
31.8
|
1.0
|
HB
|
A:THR470
|
4.2
|
30.9
|
1.0
|
HG12
|
A:VAL467
|
4.3
|
33.9
|
1.0
|
CA
|
A:CYS468
|
4.3
|
26.1
|
1.0
|
HB2
|
A:CYS468
|
4.3
|
30.8
|
1.0
|
HG21
|
A:ILE452
|
4.4
|
37.9
|
1.0
|
H
|
A:THR470
|
4.4
|
29.6
|
1.0
|
H
|
A:VAL467
|
4.4
|
33.1
|
1.0
|
H
|
A:GLN449
|
4.4
|
28.3
|
1.0
|
CB
|
A:VAL467
|
4.4
|
30.3
|
1.0
|
H
|
A:GLN451
|
4.5
|
31.2
|
1.0
|
HG1
|
A:THR470
|
4.5
|
30.4
|
1.0
|
H
|
A:ILE452
|
4.6
|
31.4
|
1.0
|
CA
|
A:CYS465
|
4.6
|
26.2
|
1.0
|
CG2
|
A:ILE452
|
4.6
|
31.6
|
1.0
|
CA
|
A:CYS447
|
4.7
|
22.5
|
1.0
|
HD11
|
A:ILE472
|
4.7
|
32.0
|
1.0
|
H
|
A:HIS469
|
4.7
|
30.2
|
1.0
|
CB
|
A:GLN449
|
4.8
|
21.7
|
1.0
|
CG1
|
A:VAL467
|
4.8
|
28.2
|
1.0
|
C
|
A:CYS450
|
4.8
|
29.8
|
1.0
|
C
|
A:GLN449
|
4.9
|
32.5
|
1.0
|
C
|
A:VAL467
|
4.9
|
33.2
|
1.0
|
N
|
A:GLN451
|
4.9
|
26.0
|
1.0
|
HA
|
A:CYS465
|
4.9
|
31.4
|
1.0
|
OG1
|
A:THR470
|
4.9
|
25.4
|
1.0
|
C
|
A:CYS468
|
4.9
|
28.3
|
1.0
|
HA
|
A:CYS450
|
4.9
|
27.6
|
1.0
|
CB
|
A:THR470
|
4.9
|
25.8
|
1.0
|
N
|
A:VAL467
|
5.0
|
27.6
|
1.0
|
HA
|
A:CYS447
|
5.0
|
27.0
|
1.0
|
CA
|
A:VAL467
|
5.0
|
27.8
|
1.0
|
|
Zinc binding site 2 out
of 6 in 9egw
Go back to
Zinc Binding Sites List in 9egw
Zinc binding site 2 out
of 6 in the Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn602
b:23.0
occ:1.00
|
SG
|
A:CYS493
|
2.3
|
20.5
|
1.0
|
SG
|
A:CYS473
|
2.3
|
21.2
|
1.0
|
SG
|
A:CYS509
|
2.4
|
23.2
|
1.0
|
SG
|
A:CYS502
|
2.4
|
20.6
|
1.0
|
HB2
|
A:CYS473
|
3.1
|
25.8
|
1.0
|
HB2
|
A:CYS495
|
3.1
|
24.7
|
1.0
|
ZN
|
A:ZN603
|
3.1
|
23.4
|
1.0
|
HB2
|
A:CYS493
|
3.2
|
24.6
|
1.0
|
HB3
|
A:CYS502
|
3.2
|
24.8
|
1.0
|
CB
|
A:CYS493
|
3.3
|
20.5
|
1.0
|
HB2
|
A:CYS509
|
3.3
|
28.1
|
1.0
|
CB
|
A:CYS502
|
3.3
|
20.7
|
1.0
|
CB
|
A:CYS473
|
3.3
|
21.5
|
1.0
|
CB
|
A:CYS509
|
3.4
|
23.4
|
1.0
|
HB2
|
A:CYS502
|
3.4
|
24.8
|
1.0
|
HB3
|
A:CYS509
|
3.5
|
28.1
|
1.0
|
HB3
|
A:CYS493
|
3.5
|
24.6
|
1.0
|
HG1
|
A:THR476
|
3.7
|
27.8
|
1.0
|
HG12
|
A:VAL475
|
3.7
|
28.3
|
1.0
|
HG23
|
A:THR476
|
3.8
|
34.7
|
1.0
|
HB3
|
A:CYS473
|
3.8
|
25.8
|
1.0
|
HD3
|
A:ARG480
|
3.9
|
24.6
|
1.0
|
HD2
|
A:ARG480
|
3.9
|
24.6
|
1.0
|
CB
|
A:CYS495
|
4.0
|
20.6
|
1.0
|
HG21
|
A:THR476
|
4.2
|
34.7
|
1.0
|
HG13
|
A:VAL475
|
4.3
|
28.3
|
1.0
|
CD
|
A:ARG480
|
4.3
|
20.5
|
1.0
|
CG1
|
A:VAL475
|
4.4
|
23.6
|
1.0
|
OG1
|
A:THR476
|
4.4
|
23.2
|
1.0
|
H
|
A:CYS495
|
4.4
|
24.9
|
1.0
|
HB3
|
A:CYS495
|
4.4
|
24.7
|
1.0
|
HA
|
A:CYS473
|
4.4
|
24.1
|
1.0
|
CG2
|
A:THR476
|
4.4
|
28.9
|
1.0
|
HG11
|
A:VAL475
|
4.5
|
28.3
|
1.0
|
CA
|
A:CYS473
|
4.5
|
20.1
|
1.0
|
NE
|
A:ARG480
|
4.6
|
21.3
|
1.0
|
SG
|
A:CYS495
|
4.6
|
22.0
|
1.0
|
H
|
A:THR476
|
4.6
|
28.0
|
1.0
|
HA
|
A:ARG480
|
4.7
|
24.0
|
1.0
|
CA
|
A:CYS493
|
4.7
|
22.9
|
1.0
|
HE
|
A:ARG480
|
4.8
|
25.6
|
1.0
|
CA
|
A:CYS502
|
4.8
|
20.2
|
1.0
|
CA
|
A:CYS509
|
4.8
|
21.7
|
1.0
|
SG
|
A:CYS506
|
4.8
|
23.8
|
1.0
|
H
|
A:CYS502
|
4.8
|
26.5
|
1.0
|
O
|
A:CYS509
|
5.0
|
23.1
|
1.0
|
N
|
A:CYS495
|
5.0
|
20.8
|
1.0
|
CA
|
A:CYS495
|
5.0
|
20.7
|
1.0
|
|
Zinc binding site 3 out
of 6 in 9egw
Go back to
Zinc Binding Sites List in 9egw
Zinc binding site 3 out
of 6 in the Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn603
b:23.4
occ:1.00
|
SG
|
A:CYS506
|
2.3
|
23.8
|
1.0
|
SG
|
A:CYS495
|
2.4
|
22.0
|
1.0
|
SG
|
A:CYS509
|
2.4
|
23.2
|
1.0
|
SG
|
A:CYS502
|
2.4
|
20.6
|
1.0
|
HB2
|
A:CYS495
|
2.9
|
24.7
|
1.0
|
ZN
|
A:ZN602
|
3.1
|
23.0
|
1.0
|
H
|
A:CYS502
|
3.2
|
26.5
|
1.0
|
CB
|
A:CYS495
|
3.2
|
20.6
|
1.0
|
HB3
|
A:CYS509
|
3.2
|
28.1
|
1.0
|
HB2
|
A:CYS506
|
3.2
|
28.5
|
1.0
|
CB
|
A:CYS506
|
3.3
|
23.8
|
1.0
|
HB3
|
A:CYS506
|
3.4
|
28.5
|
1.0
|
CB
|
A:CYS509
|
3.5
|
23.4
|
1.0
|
HB3
|
A:CYS502
|
3.5
|
24.8
|
1.0
|
H
|
A:CYS509
|
3.5
|
28.1
|
1.0
|
CB
|
A:CYS502
|
3.6
|
20.7
|
1.0
|
O
|
A:HOH705
|
3.7
|
30.5
|
1.0
|
HB3
|
A:CYS495
|
3.7
|
24.7
|
1.0
|
HG11
|
A:VAL475
|
3.9
|
28.3
|
1.0
|
N
|
A:CYS502
|
4.0
|
22.1
|
1.0
|
HB2
|
A:CYS509
|
4.2
|
28.1
|
1.0
|
N
|
A:CYS509
|
4.2
|
23.4
|
1.0
|
HH12
|
A:ARG496
|
4.3
|
49.3
|
1.0
|
HG12
|
A:VAL475
|
4.3
|
28.3
|
1.0
|
CA
|
A:CYS502
|
4.4
|
20.2
|
1.0
|
HB2
|
A:CYS502
|
4.4
|
24.8
|
1.0
|
HA
|
A:CYS495
|
4.4
|
24.9
|
1.0
|
CA
|
A:CYS509
|
4.4
|
21.7
|
1.0
|
H
|
A:HIS503
|
4.4
|
29.9
|
1.0
|
CA
|
A:CYS495
|
4.4
|
20.7
|
1.0
|
CG1
|
A:VAL475
|
4.5
|
23.6
|
1.0
|
HG13
|
A:VAL475
|
4.6
|
28.3
|
1.0
|
CA
|
A:CYS506
|
4.7
|
21.2
|
1.0
|
HA
|
A:PRO501
|
4.8
|
27.6
|
1.0
|
HA
|
A:CYS506
|
4.8
|
25.5
|
1.0
|
HB3
|
A:PRO501
|
4.8
|
31.3
|
1.0
|
SG
|
A:CYS493
|
4.8
|
20.5
|
1.0
|
NH1
|
A:ARG496
|
4.8
|
41.1
|
1.0
|
SG
|
A:CYS473
|
4.8
|
21.2
|
1.0
|
N
|
A:HIS503
|
4.9
|
24.9
|
1.0
|
HH11
|
A:ARG496
|
4.9
|
49.3
|
1.0
|
C
|
A:CYS502
|
5.0
|
23.5
|
1.0
|
|
Zinc binding site 4 out
of 6 in 9egw
Go back to
Zinc Binding Sites List in 9egw
Zinc binding site 4 out
of 6 in the Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn601
b:24.7
occ:1.00
|
SG
|
B:CYS450
|
2.3
|
24.2
|
1.0
|
SG
|
B:CYS468
|
2.3
|
24.0
|
1.0
|
SG
|
B:CYS465
|
2.3
|
25.4
|
1.0
|
SG
|
B:CYS447
|
2.3
|
26.1
|
1.0
|
HB3
|
B:CYS450
|
2.9
|
30.3
|
1.0
|
H
|
B:CYS468
|
3.1
|
30.2
|
1.0
|
H
|
B:CYS450
|
3.2
|
29.4
|
1.0
|
HB3
|
B:CYS468
|
3.2
|
33.0
|
1.0
|
HB3
|
B:CYS447
|
3.2
|
32.0
|
1.0
|
CB
|
B:CYS447
|
3.2
|
26.7
|
1.0
|
CB
|
B:CYS450
|
3.2
|
25.2
|
1.0
|
HB2
|
B:CYS447
|
3.2
|
32.0
|
1.0
|
HB3
|
B:CYS465
|
3.2
|
30.1
|
1.0
|
CB
|
B:CYS465
|
3.2
|
25.1
|
1.0
|
HB2
|
B:CYS465
|
3.3
|
30.1
|
1.0
|
CB
|
B:CYS468
|
3.3
|
27.5
|
1.0
|
N
|
B:CYS450
|
3.8
|
24.5
|
1.0
|
N
|
B:CYS468
|
3.8
|
25.2
|
1.0
|
HB3
|
B:GLN449
|
3.8
|
29.4
|
1.0
|
HB
|
B:VAL467
|
3.8
|
35.2
|
1.0
|
HG22
|
B:THR470
|
3.8
|
30.8
|
1.0
|
HB2
|
B:CYS450
|
4.0
|
30.3
|
1.0
|
HG22
|
B:ILE452
|
4.0
|
33.9
|
1.0
|
CA
|
B:CYS450
|
4.0
|
24.8
|
1.0
|
CA
|
B:CYS468
|
4.1
|
24.7
|
1.0
|
HB2
|
B:CYS468
|
4.1
|
33.0
|
1.0
|
HG21
|
B:THR470
|
4.2
|
30.8
|
1.0
|
HG21
|
B:ILE452
|
4.2
|
33.9
|
1.0
|
H
|
B:THR470
|
4.3
|
28.7
|
1.0
|
H
|
B:GLN449
|
4.4
|
31.1
|
1.0
|
CG2
|
B:THR470
|
4.5
|
25.7
|
1.0
|
H
|
B:VAL467
|
4.5
|
31.7
|
0.5
|
H
|
B:VAL467
|
4.5
|
31.7
|
0.5
|
H
|
B:GLN451
|
4.5
|
30.9
|
1.0
|
H
|
B:HIS469
|
4.6
|
29.9
|
1.0
|
H
|
B:ILE452
|
4.6
|
32.5
|
1.0
|
CG2
|
B:ILE452
|
4.6
|
28.2
|
1.0
|
CA
|
B:CYS447
|
4.6
|
27.6
|
1.0
|
HD11
|
B:ILE472
|
4.7
|
33.1
|
1.0
|
C
|
B:CYS450
|
4.7
|
34.0
|
1.0
|
CA
|
B:CYS465
|
4.7
|
25.6
|
1.0
|
CB
|
B:GLN449
|
4.7
|
24.5
|
1.0
|
C
|
B:CYS468
|
4.8
|
28.9
|
1.0
|
CB
|
B:VAL467
|
4.8
|
29.3
|
1.0
|
HB
|
B:THR470
|
4.8
|
33.1
|
1.0
|
HA
|
B:CYS450
|
4.8
|
29.8
|
1.0
|
HG12
|
B:VAL467
|
4.8
|
40.1
|
1.0
|
C
|
B:GLN449
|
4.9
|
29.7
|
1.0
|
HB
|
B:ILE452
|
4.9
|
35.3
|
1.0
|
N
|
B:HIS469
|
4.9
|
24.9
|
1.0
|
N
|
B:GLN451
|
4.9
|
25.8
|
1.0
|
C
|
B:VAL467
|
4.9
|
25.7
|
1.0
|
HA
|
B:CYS447
|
4.9
|
33.1
|
1.0
|
HA
|
B:CYS468
|
4.9
|
29.6
|
1.0
|
|
Zinc binding site 5 out
of 6 in 9egw
Go back to
Zinc Binding Sites List in 9egw
Zinc binding site 5 out
of 6 in the Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn602
b:25.6
occ:1.00
|
SG
|
B:CYS493
|
2.3
|
23.9
|
1.0
|
SG
|
B:CYS509
|
2.3
|
24.5
|
1.0
|
SG
|
B:CYS473
|
2.4
|
24.6
|
1.0
|
SG
|
B:CYS502
|
2.4
|
24.7
|
1.0
|
HB2
|
B:CYS473
|
3.0
|
30.8
|
1.0
|
HB2
|
B:CYS495
|
3.1
|
32.5
|
1.0
|
ZN
|
B:ZN603
|
3.1
|
25.8
|
1.0
|
HB2
|
B:CYS493
|
3.2
|
28.7
|
1.0
|
HB3
|
B:CYS502
|
3.2
|
29.0
|
1.0
|
CB
|
B:CYS493
|
3.3
|
23.9
|
1.0
|
CB
|
B:CYS502
|
3.3
|
24.1
|
1.0
|
CB
|
B:CYS473
|
3.3
|
25.7
|
1.0
|
HB2
|
B:CYS509
|
3.4
|
33.0
|
1.0
|
HB2
|
B:CYS502
|
3.4
|
29.0
|
1.0
|
CB
|
B:CYS509
|
3.4
|
27.5
|
1.0
|
HB3
|
B:CYS493
|
3.5
|
28.7
|
1.0
|
HB3
|
B:CYS509
|
3.5
|
33.0
|
1.0
|
HG1
|
B:THR476
|
3.7
|
34.1
|
1.0
|
HD3
|
B:ARG480
|
3.8
|
27.9
|
1.0
|
HG12
|
B:VAL475
|
3.8
|
37.4
|
1.0
|
HB3
|
B:CYS473
|
3.8
|
30.8
|
1.0
|
HD2
|
B:ARG480
|
3.8
|
27.9
|
1.0
|
HG23
|
B:THR476
|
3.9
|
37.7
|
1.0
|
CB
|
B:CYS495
|
4.0
|
27.1
|
1.0
|
HG13
|
B:VAL475
|
4.1
|
37.4
|
1.0
|
CD
|
B:ARG480
|
4.2
|
23.2
|
1.0
|
CG1
|
B:VAL475
|
4.3
|
31.1
|
1.0
|
H
|
B:CYS495
|
4.3
|
28.9
|
0.6
|
H
|
B:CYS495
|
4.3
|
28.9
|
0.4
|
HA
|
B:CYS473
|
4.3
|
29.4
|
1.0
|
HG21
|
B:THR476
|
4.3
|
37.7
|
1.0
|
OG1
|
B:THR476
|
4.4
|
28.4
|
1.0
|
HB3
|
B:CYS495
|
4.4
|
32.5
|
1.0
|
HG11
|
B:VAL475
|
4.4
|
37.4
|
1.0
|
CA
|
B:CYS473
|
4.5
|
24.5
|
1.0
|
NE
|
B:ARG480
|
4.5
|
23.3
|
1.0
|
CG2
|
B:THR476
|
4.5
|
31.4
|
1.0
|
SG
|
B:CYS495
|
4.6
|
24.5
|
1.0
|
H
|
B:THR476
|
4.7
|
34.0
|
1.0
|
HE
|
B:ARG480
|
4.7
|
28.0
|
1.0
|
CA
|
B:CYS493
|
4.7
|
25.0
|
1.0
|
HA
|
B:ARG480
|
4.7
|
27.2
|
1.0
|
CA
|
B:CYS502
|
4.8
|
24.4
|
1.0
|
H
|
B:CYS502
|
4.8
|
31.6
|
1.0
|
SG
|
B:CYS506
|
4.8
|
28.6
|
1.0
|
CA
|
B:CYS509
|
4.9
|
25.8
|
1.0
|
N
|
B:CYS495
|
5.0
|
24.1
|
1.0
|
H
|
B:CYS493
|
5.0
|
28.2
|
1.0
|
|
Zinc binding site 6 out
of 6 in 9egw
Go back to
Zinc Binding Sites List in 9egw
Zinc binding site 6 out
of 6 in the Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Hoil-1 RING2 Domain Bound to Ubiquitin-Maltose (Maltose Not Modelled) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn603
b:25.8
occ:1.00
|
SG
|
B:CYS506
|
2.3
|
28.6
|
1.0
|
SG
|
B:CYS509
|
2.4
|
24.5
|
1.0
|
SG
|
B:CYS502
|
2.4
|
24.7
|
1.0
|
SG
|
B:CYS495
|
2.4
|
24.5
|
1.0
|
HB2
|
B:CYS495
|
2.8
|
32.5
|
1.0
|
H
|
B:CYS502
|
3.1
|
31.6
|
1.0
|
ZN
|
B:ZN602
|
3.1
|
25.6
|
1.0
|
CB
|
B:CYS495
|
3.2
|
27.1
|
1.0
|
HB3
|
B:CYS509
|
3.2
|
33.0
|
1.0
|
HB2
|
B:CYS506
|
3.3
|
37.0
|
1.0
|
CB
|
B:CYS506
|
3.3
|
30.8
|
1.0
|
H
|
B:CYS509
|
3.4
|
34.3
|
1.0
|
CB
|
B:CYS509
|
3.4
|
27.5
|
1.0
|
HB3
|
B:CYS506
|
3.5
|
37.0
|
1.0
|
HB3
|
B:CYS502
|
3.5
|
29.0
|
1.0
|
CB
|
B:CYS502
|
3.6
|
24.1
|
1.0
|
HB3
|
B:CYS495
|
3.6
|
32.5
|
1.0
|
O
|
B:HOH757
|
3.7
|
30.0
|
1.0
|
N
|
B:CYS502
|
3.9
|
26.3
|
1.0
|
HG11
|
B:VAL475
|
4.0
|
37.4
|
1.0
|
N
|
B:CYS509
|
4.0
|
28.6
|
1.0
|
O
|
B:HOH706
|
4.1
|
38.2
|
1.0
|
HB2
|
B:CYS509
|
4.2
|
33.0
|
1.0
|
CA
|
B:CYS502
|
4.3
|
24.4
|
1.0
|
CA
|
B:CYS509
|
4.3
|
25.8
|
1.0
|
HB2
|
B:CYS502
|
4.3
|
29.0
|
1.0
|
HA
|
B:CYS495
|
4.4
|
30.1
|
1.0
|
HG12
|
B:VAL475
|
4.4
|
37.4
|
1.0
|
CA
|
B:CYS495
|
4.4
|
25.1
|
1.0
|
H
|
B:HIS503
|
4.5
|
30.7
|
1.0
|
CG1
|
B:VAL475
|
4.5
|
31.1
|
1.0
|
HE
|
B:ARG496
|
4.6
|
49.3
|
1.0
|
HG13
|
B:VAL475
|
4.6
|
37.4
|
1.0
|
CA
|
B:CYS506
|
4.7
|
31.5
|
1.0
|
SG
|
B:CYS493
|
4.7
|
23.9
|
1.0
|
HA
|
B:PRO501
|
4.7
|
30.1
|
1.0
|
HB3
|
B:PRO501
|
4.7
|
35.2
|
1.0
|
HA
|
B:CYS506
|
4.9
|
37.8
|
1.0
|
SG
|
B:CYS473
|
4.9
|
24.6
|
1.0
|
N
|
B:HIS503
|
4.9
|
25.6
|
1.0
|
C
|
B:CYS502
|
5.0
|
26.4
|
1.0
|
|
Reference:
X.S.Wang,
J.Jiou,
A.Cerra,
S.A.Cobbold,
M.Jochem,
K.H.T.Mak,
L.Corcilius,
R.J.Payne,
E.D.Goddard-Borger,
D.Komander,
B.C.Lechtenberg.
The Rbr E3 Ubiquitin Ligase Hoil-1 Can Ubiquitinate Diverse Non-Protein Substrates in Vitro Biorxiv 2024.
ISSN: ISSN 2692-8205
Page generated: Sun Dec 15 12:16:50 2024
|