129l
From PDBWiki
STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT
| Authors | Pjura, P. Matthews, B.W. |
| Citation | Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent. |
| Release date | 1994-01-31 |
| Exp. Method | X-RAY DIFFRACTION |
| Resolution | 1.7 Å |
| Classification | HYDROLASE(O-GLYCOSYL) |
Sequence
Chain A (164 residues): Blast Uniprot EC 3.2.1.17MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDTVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA YKNL
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