Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1NDD

STRUCTURE OF NEDD8

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0006357biological_processregulation of transcription by RNA polymerase II
A0006508biological_processproteolysis
A0006511biological_processubiquitin-dependent protein catabolic process
A0008104biological_processprotein localization
A0009653biological_processanatomical structure morphogenesis
A0016567biological_processprotein ubiquitination
A0019941biological_processmodification-dependent protein catabolic process
A0030162biological_processregulation of proteolysis
A0031386molecular_functionprotein tag activity
A0031625molecular_functionubiquitin protein ligase binding
A0036211biological_processprotein modification process
A0045116biological_processprotein neddylation
A0070062cellular_componentextracellular exosome
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
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005829cellular_componentcytosol
C0006357biological_processregulation of transcription by RNA polymerase II
C0006508biological_processproteolysis
C0006511biological_processubiquitin-dependent protein catabolic process
C0008104biological_processprotein localization
C0009653biological_processanatomical structure morphogenesis
C0016567biological_processprotein ubiquitination
C0019941biological_processmodification-dependent protein catabolic process
C0030162biological_processregulation of proteolysis
C0031386molecular_functionprotein tag activity
C0031625molecular_functionubiquitin protein ligase binding
C0036211biological_processprotein modification process
C0045116biological_processprotein neddylation
C0070062cellular_componentextracellular exosome
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005829cellular_componentcytosol
D0006357biological_processregulation of transcription by RNA polymerase II
D0006508biological_processproteolysis
D0006511biological_processubiquitin-dependent protein catabolic process
D0008104biological_processprotein localization
D0009653biological_processanatomical structure morphogenesis
D0016567biological_processprotein ubiquitination
D0019941biological_processmodification-dependent protein catabolic process
D0030162biological_processregulation of proteolysis
D0031386molecular_functionprotein tag activity
D0031625molecular_functionubiquitin protein ligase binding
D0036211biological_processprotein modification process
D0045116biological_processprotein neddylation
D0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 2001
ChainResidue
BLEU171
BHOH1036
CLEU271

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 2002
ChainResidue
ALEU71
AHOH1054
DLEU371
DHOH1068

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 3001
ChainResidue
DARG342
DGLN349
DHOH1043
DLYS327
DGLN341

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 3002
ChainResidue
ASER46
CASN251
CLYS254
CHOH1088

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 3003
ChainResidue
CLYS227
CARG242
CHOH1008
CHOH1038

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 3004
ChainResidue
ALYS48
AGLN49
CLYS248
CLYS260

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KerVeEkegIPpqqQrLIYsGkqmnD
ChainResidueDetails
ALYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsSITE: Interaction with UBE1C => ECO:0000269|PubMed:14690597
ChainResidueDetails
ALEU8
AILE44
BLEU108
BILE144
CLEU208
CILE244
DLEU308
DILE344

site_idSWS_FT_FI2
Number of Residues4
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
AGLN40
BGLN140
CGLN240
DGLN340

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P29595
ChainResidueDetails
ALYS48
BLYS148
CLYS248
DLYS348

site_idSWS_FT_FI4
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
AGLY76
BGLY176
CGLY276
DGLY376

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon