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1XT9

Crystal Structure of Den1 in complex with Nedd8

Functional Information from GO Data
ChainGOidnamespacecontents
A0000338biological_processprotein deneddylation
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
A0016579biological_processprotein deubiquitination
A0019784molecular_functiondeNEDDylase activity
A0043687biological_processpost-translational protein modification
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005829cellular_componentcytosol
B0006357biological_processregulation of transcription by RNA polymerase II
B0006508biological_processproteolysis
B0006511biological_processubiquitin-dependent protein catabolic process
B0008104biological_processprotein localization
B0009653biological_processanatomical structure morphogenesis
B0016567biological_processprotein ubiquitination
B0019941biological_processmodification-dependent protein catabolic process
B0030162biological_processregulation of proteolysis
B0031386molecular_functionprotein tag activity
B0031625molecular_functionubiquitin protein ligase binding
B0036211biological_processprotein modification process
B0045116biological_processprotein neddylation
B0070062cellular_componentextracellular exosome
B0098978cellular_componentglutamatergic synapse
B0150052biological_processregulation of postsynapse assembly
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KerVeEkegIPpqqQrLIYsGkqmnD
ChainResidueDetails
BLYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Interaction with UBE1C => ECO:0000269|PubMed:14690597
ChainResidueDetails
BLEU8
BILE44

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: (Microbial infection) Deamidated glutamine => ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597
ChainResidueDetails
BGLN40

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P29595
ChainResidueDetails
BLYS48

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
BGLY76

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bkr
ChainResidueDetails
ATRP103
AHIS102
AASP119
ATRP26
ACYS163

site_idMCSA1
Number of Residues5
DetailsM-CSA 820
ChainResidueDetails
ATRP26electrostatic stabiliser
AHIS102proton acceptor, proton donor
ATRP103electrostatic stabiliser
AASP119electrostatic stabiliser
ACYS163nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-11-20

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