AMSH-like protease
Homo sapiens
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain A; UniProt 263–436 | Not recorded | Ubiquitin variant × 1 ZN ZINC ION × 2 EDO 1,2-ETHANEDIOL × 2 SO4 SULFATE ION × 2 UNX UNKNOWN LIGAND × 2 | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;291 K;20% PEG 1500, 0.2M NaCl, 0.1M HEPES pH7.5 | Resolution 2.01 Å R-free 0.214 |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | STALP_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 2–175; UniProt 263–436 |