› › Function and Biology

C-terminal cysteine-rich domain of human CHFR bound to mADPr

Source organism: Homo sapiens
Biochemical function: not assigned
Biological process: not assigned
Cellular component: not assigned

Quick links

EC 2.3.2.27: RING-type E3 ubiquitin transferase

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Systematic name:
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein]-L-lysine ubiquitin transferase (isopeptide bond-forming; RING-type)
Alternative Name(s):
  • RING E3 ligase
  • Ubiquitin transferase RING E3

GO terms

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF17979
Domain description: Cysteine rich domain with multizinc binding regions
Occurring in:
  1. E3 ubiquitin-protein ligase CHFR
The deposited structure of PDB entry 2xoc contains 2 copies of Pfam domain PF17979 (Cysteine rich domain with multizinc binding regions) in E3 ubiquitin-protein ligase CHFR. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR019406
Domain description: Aprataxin and PNK-like factor, PBZ domain
Occurring in:
  1. E3 ubiquitin-protein ligase CHFR
IPR040909
Domain description: E3 ubiquitin-protein ligase CHFR, cysteine rich domain with multizinc binding
Occurring in:
  1. E3 ubiquitin-protein ligase CHFR

Structure domain

CATH CATH domain
3.30.40.140
Class: Alpha Beta
Architecture: 2-Layer Sandwich
Topology: Herpes Virus-1
Homology: Herpes Virus-1
Occurring in:
  1. E3 ubiquitin-protein ligase CHFR
The deposited structure of PDB entry 2xoc contains 2 copies of CATH domain 3.30.40.140 (Herpes Virus-1) in E3 ubiquitin-protein ligase CHFR. Showing 1 copy in chain A.

Quick links