Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6PGR

Cocomplex structure of Deoxyhypusine synthase with inhibitor 6-BROMO-N-(1H-INDOL-4-YL)-1-BENZOTHIOPHENE-2-CARBOXAMIDE

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
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
B0042802molecular_functionidentical protein binding
B0046203biological_processspermidine catabolic process
B0051604biological_processprotein maturation
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue 8XY A 401
ChainResidue
ATYR103
BASP238
AVAL129
AILE266
AASN267
ALEU281
AGLY284
AVAL286
AHIS288
ALYS329

site_idAC2
Number of Residues10
Detailsbinding site for residue 8XY B 401
ChainResidue
AASP238
BTYR103
BVAL129
BILE266
BASN267
BLEU281
BGLY284
BVAL286
BHIS288
BLYS329

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 Residues1
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
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

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon