8CQF
Crystal Structure of a Chimeric Alpha-Amylase from Pseudoalteromonas Haloplanktis Complexed with Rearranged Acarbose
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Alpha-amylase | polymer | 450 | 49225.0 | 1 | UniProt (P29957) | Pseudoalteromonas haloplanktis | 1,4-alpha-D-glucan glucanohydrolase |
| 2 | B, D (D, C) | 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose | branched | 645.6 | 2 | In PDB GlyTouCan (G66431MI) | |||
| 3 | C (B) | 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-1,5-anhydro-D-glucitol | branched | 467.5 | 1 | In PDB GlyTouCan (G87323JT) | |||
| 4 | E (E) | alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose | branched | 807.7 | 1 | In PDB GlyTouCan (G15322CN) | |||
| 5 | F, G (A) | CHLORIDE ION | non-polymer | 35.5 | 2 | Chemie (CL) | |||
| 6 | H (A) | CALCIUM ION | non-polymer | 40.1 | 1 | Chemie (CA) | |||
| 7 | I (A) | 1,2-ETHANEDIOL | non-polymer | 62.1 | 1 | Chemie (EDO) | |||
| 8 | J (A) | water | water | 18.0 | 297 | Chemie (HOH) |
Sequence modifications
A: 2 - 208 (UniProt: P29957)
A: 212 - 270 (UniProt: P29957)
A: 278 - 448 (UniProt: P29957)
| PDB | External Database | Details |
|---|---|---|
| His 1 | - | expression tag |
| Val 77 | Ala 101 | engineered mutation |
| Leu 204 | Gln 228 | engineered mutation |
| PDB | External Database | Details |
|---|---|---|
| Ile 209 | - | linker |
| Lys 210 | - | linker |
| Ser 211 | - | linker |
| Gly 226 | Ser 250 | engineered mutation |
| Ala 227 | Thr 251 | engineered mutation |
| Lys 228 | Glu 252 | engineered mutation |
| Thr 231 | Asn 255 | engineered mutation |
| Val 232 | Thr 256 | engineered mutation |
| PDB | External Database | Details |
|---|---|---|
| Ala 271 | - | linker |
| Gly 272 | - | linker |
| Gly 273 | - | linker |
| Ser 274 | - | linker |
| Ser 275 | - | linker |
| Ile 276 | - | linker |
| Leu 277 | - | linker |
| Arg 301 | Lys 324 | engineered mutation |
| Asn 311 | Asp 334 | engineered mutation |
| Asp 312 | Thr 335 | engineered mutation |
| Trp 313 | Asp 336 | engineered mutation |
| Gly 449 | - | expression tag |
| Ala 450 | - | expression tag |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 49225.0 | |
| Branched | Number of molecules | 4 |
| Total formula weight | 2566.4 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 173.1 | |
| All* | Total formula weight | 51964.5 |
