169l
From PDBWiki
PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME
| Authors | Zhang, X.J. Wozniak, J.A. Matthews, B.W. |
| Citation | Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme. |
| Release date | 2003-04-01 |
| Exp. Method | X-RAY DIFFRACTION |
| Resolution | 3.0 Å |
| Classification | HYDROLASE (O-GLYCOSYL) |
Sequence
Chain A (164 residues): Blast Uniprot EC 3.2.1.17MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDAAAAALAAAAWAAATPNRAKRVITTFRTGTWDA YKNLChain B (164 residues): Blast Uniprot EC 3.2.1.17
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDAAAAALAAAAWAAATPNRAKRVITTFRTGTWDA YKNLChain C (164 residues): Blast Uniprot EC 3.2.1.17
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDAAAAALAAAAWAAATPNRAKRVITTFRTGTWDA YKNLChain D (164 residues): Blast Uniprot EC 3.2.1.17
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDAAAAALAAAAWAAATPNRAKRVITTFRTGTWDA YKNLChain E (164 residues): Blast Uniprot EC 3.2.1.17
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDAAAAALAAAAWAAATPNRAKRVITTFRTGTWDA YKNL
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