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MineSummary [1gb0]

Summary Structural Experimental Function Sequence Neighbor Download Link

<Asymmetric unit>
= <Biological unit>

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( jV3 / Jmol ) *1
PDB ID1gb0  sequence information (FASTA format)   
RELATED PDB ID2mei, 1gay, 1gaz, 1gb2, 1gb3, 1gb5, 1gb7, 1gb8, 1gb9, 1gbo, 1gbw, 1gbx, 1gby, 1gbz
DescriptorLYSOZYME
TitleCRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
Functional Keywordssurface mutant, HYDROLASE
Biological sourceHomo sapiens (human)
Organ source [UNP - P61626] Colon
[UNP - P61626] Urine
[UNP - P61626] Milk
Total number of polymer chains1
Total molecular weight14757.8 (the details in Structural Details Page)
AuthorsFunahashi, J. , Takano, K. , Yamagata, Y. , Yutani, K. (deposition date : 2000-06-26, release date : 2000-07-27)
Primary citationFunahashi, J. , Takano, K. , Yamagata, Y. , Yutani, K.
Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions.
Biochemistry, 39:14448 - 14456, 2000.(PubMed : 11087397)  (DOI: 10.1021/bi0015717)
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