2ZEH
Crystal structure of the human glutaminyl cyclase mutant E201Q at 1.8 angstrom resolution
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B | Glutaminyl-peptide cyclotransferase | polymer | 329 | 37556.4 | 2 | UniProt (Q16769) Pfam (PF04389) In PDB | Homo sapiens (human) | QC, Glutaminyl-tRNA cyclotransferase, Glutaminyl cyclase, Glutamyl cyclase |
| 2 | A, B | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
| 3 | A, B | SULFATE ION | non-polymer | 96.1 | 2 | Chemie (SO4) | |||
| 4 | water | water | 18.0 | 867 | Chemie (HOH) |
Sequence modifications
A, B: 33 - 361 (UniProt: Q16769)
| PDB | External Database | Details |
|---|---|---|
| Gln 201 | Glu 201 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 75112.8 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 322.9 | |
| All* | Total formula weight | 75435.8 |
