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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>
= <Biological unit>

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PDB ID1ugd  sequence information (FASTA format)   
DescriptorCARBONIC ANHYDRASE II
TitleHUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)
Functional KeywordsLYASE (OXO-ACID), ACETYLATION, ZINC, POLYMORPHISM, DISEASE MUTATION
Biological sourceHomo sapiens (human)
Cellular location [UNP - P00918] Cytoplasm
Organ source [UNP - P00918] Ovary
Total number of polymer chains1
Total molecular weight29152.4 (the details in Structural Details Page)
AuthorsScolnick, L.R. , Christianson, D.W. (deposition date : 1996-07-24, release date : 1997-01-27)
Primary citationScolnick, L.R. , Christianson, D.W.
X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis.
Biochemistry, 35:16429 - 16434, 1996.(PubMed : 8987974)  (DOI: 10.1021/bi9617872)
Experimental methodX-RAY DIFFRACTION ( 2.0[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P00918 ) , eF-site , KEGG ( EC 4.2.1.1 ) , PISA