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7A6T

Crystal Structure of Asn173Ser variant of Human Deoxyhypusine Synthase in complex with NAD and spermidine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0008216biological_processspermidine metabolic process
A0008284biological_processpositive regulation of cell population proliferation
A0008612biological_processpeptidyl-lysine modification to peptidyl-hypusine
A0016740molecular_functiontransferase activity
A0034038molecular_functiondeoxyhypusine synthase activity
A0042102biological_processpositive regulation of T cell proliferation
A0042593biological_processglucose homeostasis
A0042802molecular_functionidentical protein binding
A0046203biological_processspermidine catabolic process
A0051604biological_processprotein maturation
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0008216biological_processspermidine metabolic process
B0008284biological_processpositive regulation of cell population proliferation
B0008612biological_processpeptidyl-lysine modification to peptidyl-hypusine
B0016740molecular_functiontransferase activity
B0034038molecular_functiondeoxyhypusine synthase activity
B0042102biological_processpositive regulation of T cell proliferation
B0042593biological_processglucose homeostasis
B0042802molecular_functionidentical protein binding
B0046203biological_processspermidine catabolic process
B0051604biological_processprotein maturation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9405486","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9493264","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues22
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 687
ChainResidueDetails
AGLU137electrostatic stabiliser
AASN292proton acceptor, proton donor
AASP333covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 687
ChainResidueDetails
BGLU137electrostatic stabiliser
BASN292proton acceptor, proton donor
BASP333covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

240971

PDB entries from 2025-08-27

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