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3UGK

Crystal Structure of C205S mutant and Saccharopine Dehydrogenase from Saccharomyces cerevisiae.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003729molecular_functionmRNA binding
A0004753molecular_functionsaccharopine dehydrogenase activity
A0004754molecular_functionsaccharopine dehydrogenase (NAD+, L-lysine-forming) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0008652biological_processamino acid biosynthetic process
A0009085biological_processlysine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016558biological_processprotein import into peroxisome matrix
A0019878biological_processlysine biosynthetic process via aminoadipic acid
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMotif: {"description":"Microbody targeting signal","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10077615","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"22243403","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17939687","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"22243403","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17939687","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22243403","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17939687","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3UH1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3UH1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3UHA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22243403","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17939687","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3UH1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UHA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22243403","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UH1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UHA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine; partial","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Peters C."]}}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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