1RP9
Crystal structure of barley alpha-amylase isozyme 1 (amy1) inactive mutant d180a in complex with acarbose
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | Alpha-amylase type 1 isozyme | polymer | 405 | 44596.0 | 1 | UniProt (P00693) Pfam (PF00128) Pfam (PF07821) In PDB | Hordeum vulgare | 1,4-alpha-D-glucan glucanohydrolase, AMY1, Low pI alpha-amylase |
| 2 | B | 4,6-dideoxy-4-{[(1S,5R,6S)-3-formyl-5,6-dihydroxy-4-oxocyclohex-2-en-1-yl]amino}-alpha-D-xylo-hex-5-enopyranose-(1-4)-beta-D-glucopyranose-(1-4)-alpha-D-glucopyranose | branched | 639.6 | 1 | ||||
| 3 | C, D | 4,6-dideoxy-4-{[(1S,5R,6S)-3-formyl-5,6-dihydroxy-4-oxocyclohex-2-en-1-yl]amino}-alpha-D-xylo-hex-5-enopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose | branched | 639.6 | 2 | ||||
| 4 | A | CALCIUM ION | non-polymer | 40.1 | 3 | Chemie (CA) | |||
| 5 | water | water | 18.0 | 396 | Chemie (HOH) |
Sequence modifications
A: 1 - 405 (UniProt: P00693)
| PDB | External Database | Details |
|---|---|---|
| Ala 180 | Asp 204 | engineered mutation |
| Val 284 | Ala 308 | SEE REMARK 999 |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 44596.0 | |
| Branched | Number of molecules | 3 |
| Total formula weight | 1918.7 | |
| Non-Polymers* | Number of molecules | 3 |
| Total formula weight | 120.2 | |
| All* | Total formula weight | 46635.0 |
