2XTU
Structure of E.coli rhomboid protease GlpG active site mutant, S201T in trigonal crystal form
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A | RHOMBOID PROTEASE GLPG | polymer | 181 | 20471.3 | 1 | UniProt (P09391) Pfam (PF01694) In PDB | ESCHERICHIA COLI | GLPG, INTRAMEMBRANE SERINE PROTEASE |
2 | A | nonyl beta-D-glucopyranoside | non-polymer | 306.4 | 18 | Chemie (BNG) | |||
3 | water | water | 18.0 | 87 | Chemie (HOH) |
Sequence modifications
A: 91 - 271 (UniProt: P09391)
PDB | External Database | Details |
---|---|---|
Thr 201 | Ser 201 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 1 |
Total formula weight | 20471.3 | |
Non-Polymers* | Number of molecules | 18 |
Total formula weight | 5515.1 | |
All* | Total formula weight | 25986.4 |