7F5J
The crystal structure of VyPAL2-I244V, a more efficient mutant of VyPAL2 peptide asparaginyl ligase in its active enzyme form
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | Peptide Asparaginyl Ligases | polymer | 282 | 31118.8 | 2 | UniProt (A0A509GV09) Pfam (PF01650) | Viola philippica | |
| 2 | C (C) | alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 367.3 | 1 | In PDB GlyTouCan (G86851RC) | |||
| 3 | D (D) | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | branched | 424.4 | 1 | In PDB GlyTouCan (G42666HT) | |||
| 4 | E, H, N, P (A, B) | 2-acetamido-2-deoxy-beta-D-glucopyranose | non-polymer | 221.2 | 4 | Chemie (NAG) | |||
| 5 | F, G, I, K, Q... (A, B) | 1,2-ETHANEDIOL | non-polymer | 62.1 | 6 | Chemie (EDO) | |||
| 6 | J, L, M, O (A, B) | GLYCEROL | non-polymer | 92.1 | 4 | Chemie (GOL) | |||
| 7 | S, T (A, B) | water | water | 18.0 | 500 | Chemie (HOH) |
Sequence modifications
A, B: 50 - 332 (UniProt: A0A509GV09)
| PDB | External Database | Details |
|---|---|---|
| - | Asp 171 | deletion |
| Hd0 172 | His 172 | conflict |
| Val 244 | Ile 244 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 62237.6 | |
| Branched | Number of molecules | 2 |
| Total formula weight | 791.8 | |
| Non-Polymers* | Number of molecules | 14 |
| Total formula weight | 1625.6 | |
| All* | Total formula weight | 64655.0 |
