3RII
Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B | Ubiquitin carboxyl-terminal hydrolase isozyme L5 | polymer | 233 | 26329.9 | 2 | UniProt (Q9Y5K5) Pfam (PF01088) In PDB | Homo sapiens (human) | UCH-L5, Ubiquitin C-terminal hydrolase UCH37, Ubiquitin thioesterase L5 |
2 | A, B | 1,2-ETHANEDIOL | non-polymer | 62.1 | 2 | Chemie (EDO) | |||
3 | A | MAGNESIUM ION | non-polymer | 24.3 | 1 | Chemie (MG) | |||
4 | water | water | 18.0 | 278 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 228 (UniProt: Q9Y5K5)
PDB | External Database | Details |
---|---|---|
Gly -4 | - | EXPRESSION TAG |
Pro -3 | - | EXPRESSION TAG |
Leu -2 | - | EXPRESSION TAG |
Gly -1 | - | EXPRESSION TAG |
Ser 0 | - | EXPRESSION TAG |
Ser 88 | Cys 88 | ENGINEERED MUTATION |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 52659.7 | |
Non-Polymers* | Number of molecules | 3 |
Total formula weight | 148.4 | |
All* | Total formula weight | 52808.2 |