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7A6S

Crystal Structure of Asn173Ser variant of Human Deoxyhypusine Synthase

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
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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:9405486
ChainResidueDetails
ALYS329
BLYS329

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:9493264
ChainResidueDetails
ASER105
BGLU137
BASP238
BGLY283
BTHR308
BASP342
ATHR131
AGLU137
AASP238
AGLY283
ATHR308
AASP342
BSER105
BTHR131

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AGLU136
BGLU323
AASP243
AHIS288
AGLY314
AGLU323
BGLU136
BASP243
BHIS288
BGLY314

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER78
BSER78

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 687
ChainResidueDetails
AGLU137electrostatic stabiliser
AHIS288proton acceptor, proton donor
ALYS329covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 687
ChainResidueDetails
BGLU137electrostatic stabiliser
BHIS288proton acceptor, proton donor
BLYS329covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-07-10

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