1HL2
Crystal structure of N-acetylneuraminate lyase from E. coli mutant L142R in complex with b-hydroxypyruvate
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B, C, D | N-ACETYLNEURAMINATE LYASE SUBUNIT | polymer | 297 | 32670.4 | 4 | UniProt (P06995) Pfam (PF00701) UniProt (by SIFTS) (P0A6L4) In PDB | ESCHERICHIA COLI | N-ACETYLNEURAMINIC ACID ALDOLASE, N-ACETYLNEURAMINATE PYRUVATE LYASE, NALASE |
2 | A, B, C, D | 3-HYDROXYPYRUVIC ACID | non-polymer | 104.1 | 4 | Chemie (3PY) | |||
3 | water | water | 18.0 | 832 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 1 - 1 (PDB: 1HL2)
A, B, C, D: 2 - 297 (UniProt: P06995)
A, B, C, D: 2 - 297 (UniProt: P06995)
PDB | External Database | Details |
---|---|---|
Arg 142 | Leu 141 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 4 |
Total formula weight | 130681.6 | |
Non-Polymers* | Number of molecules | 4 |
Total formula weight | 416.2 | |
All* | Total formula weight | 131097.9 |