English Statistics Help FAQ Contact Us
Download >>

PDBj (Protein Data Bank Japan) maintains a centralized PDB archive of macromolecular structures and provides integrated tools, in collaboration with the RCSB, the BMRB in USA and the PDBe in EU. PDBj is supported by JST-NBDC and Osaka University.

Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>
= <Biological unit>

More images...
View in 3D molecule viewer
( jV3 / Jmol ) *1
PDB ID1oue  sequence information (FASTA format)   
DescriptorLYSOZYME
TitleCONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V125A MUTANT
Functional KeywordsHYDROLASE (O-GLYCOSYL), SIGNAL, AMYLOID, DISEASE MUTATION
Biological sourceHomo sapiens (human)
Organ source [UNP - P61626] Colon
[UNP - P61626] Urine
[UNP - P61626] Milk
Total number of polymer chains1
Total molecular weight14715.7 (the details in Structural Details Page)
AuthorsTakano, K. , Yamagata, Y. , Fujii, S. , Yutani, K. (deposition date : 1996-08-23, release date : 1997-02-12)
Primary citationTakano, K. , Yamagata, Y. , Fujii, S. , Yutani, K.
Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants.
Biochemistry, 36:688 - 698, 1997.(PubMed : 9020766)  (DOI: 10.1021/bi9621829)
Experimental methodX-RAY DIFFRACTION ( 1.8[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P61626 ) , eF-site , KEGG ( EC 3.2.1.17 ) , PISA