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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:

Chlorine (Cl) 1 atom

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: Fri Aug 22 17:15:28 2025

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