9HO1
Room temperature structure of Aspartyl/Asparaginyl beta-hydroxylase (AspH) in complex with Fe, 2-oxoglutarate, and hydroxylated Factor X derived peptide fragment, 1.5 s O2 exposure
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Aspartyl/asparaginyl beta-hydroxylase | polymer | 429 | 49405.3 | 1 | UniProt (Q12797) | Homo sapiens (human) | Aspartate beta-hydroxylase,ASP beta-hydroxylase,Peptide-aspartate beta-dioxygenase |
| 2 | B (B) | Factor X light chain | polymer | 39 | 4206.4 | 1 | UniProt (P00742) | Homo sapiens | |
| 3 | C (A) | 2-OXOGLUTARIC ACID | non-polymer | 146.1 | 1 | Chemie (AKG) | |||
| 4 | D (A) | SUCCINIC ACID | non-polymer | 118.1 | 1 | Chemie (SIN) | |||
| 5 | E (A) | FE (III) ION | non-polymer | 55.8 | 1 | Chemie (FE) | |||
| 6 | F, G (A, B) | water | water | 18.0 | 169 | Chemie (HOH) |
Sequence modifications
B: 86 - 124 (UniProt: P00742)
| PDB | External Database | Details |
|---|---|---|
| Ser 90 | Cys 90 | engineered mutation |
| Ser 95 | Cys 95 | engineered mutation |
| Ser 112 | Cys 112 | engineered mutation |
| Ser 121 | Cys 121 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 53611.7 | |
| Non-Polymers* | Number of molecules | 3 |
| Total formula weight | 320.0 | |
| All* | Total formula weight | 53931.8 |
