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4F8C

Structure of the Cif:Nedd8 complex - Yersinia pseudotuberculosis Cycle Inhibiting Factor in complex with human Nedd8

Functional Information from GO Data
ChainGOidnamespacecontents
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
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 Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 301
ChainResidue
ALEU57
AASN60
AVAL61
ASER108
ASER109
AARG111
AHOH510

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AILE235
AASP236
AHIS239
AILE240
AHIS226
AGLY229

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 301
ChainResidue
CTHR225
CHIS226
CILE235
CASP236
CHIS239
CILE240

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 302
ChainResidue
CLEU57
CASN60
CVAL61
CSER108
CARG111
CHOH530

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
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:19308257, ECO:0000305|PubMed:22691497
ChainResidueDetails
AALA117
CALA117
DLEU8
DILE44

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q63KH5
ChainResidueDetails
AHIS173
AGLN193
CHIS173
CGLN193

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P29595
ChainResidueDetails
BLYS48
DLYS48

site_idSWS_FT_FI4
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
BGLY76
DGLY76

222926

PDB entries from 2024-07-24

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