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3UHA

Crystal Structure of Saccharopine Dehydrogenase from Saccharomyces cervisiae complexed with NAD.

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
B0003729molecular_functionmRNA binding
B0004753molecular_functionsaccharopine dehydrogenase activity
B0004754molecular_functionsaccharopine dehydrogenase (NAD+, L-lysine-forming) activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005777cellular_componentperoxisome
B0008652biological_processamino acid biosynthetic process
B0009085biological_processlysine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016558biological_processprotein import into peroxisome matrix
B0019878biological_processlysine biosynthetic process via aminoadipic acid
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NAD A 374
ChainResidue
AARG130
ATHR231
AILE250
ATYR251
AILE256
AVAL278
AILE318
AASP319
AHIS320
ALEU321
APRO322
AALA139
AILE199
AGLY200
AGLY203
AARG204
ASER205
AASP227
AILE228

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAD B 374
ChainResidue
BARG130
BALA139
BILE199
BGLY200
BGLY203
BARG204
BSER205
BASP227
BILE228
BTHR231
BCYS249
BILE250
BTYR251
BILE256
BVAL278
BILE318
BASP319
BHIS320
BLEU321
BPRO322
BHOH377

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 375
ChainResidue
ALYS193
BLYS193

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"22243403","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17939687","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"22243403","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17939687","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
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_FI4
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3UH1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"3UHA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
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_FI7
Number of Residues8
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

247536

PDB entries from 2026-01-14

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