4F8C
Structure of the Cif:Nedd8 complex - Yersinia pseudotuberculosis Cycle Inhibiting Factor in complex with human Nedd8
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
B | 0006508 | biological_process | proteolysis |
B | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
B | 0008104 | biological_process | protein localization |
B | 0009653 | biological_process | anatomical structure morphogenesis |
B | 0016567 | biological_process | protein ubiquitination |
B | 0019941 | biological_process | modification-dependent protein catabolic process |
B | 0030162 | biological_process | regulation of proteolysis |
B | 0031386 | molecular_function | protein tag activity |
B | 0031625 | molecular_function | ubiquitin protein ligase binding |
B | 0036211 | biological_process | protein modification process |
B | 0045116 | biological_process | protein neddylation |
B | 0070062 | cellular_component | extracellular exosome |
D | 0005515 | molecular_function | protein binding |
D | 0005634 | cellular_component | nucleus |
D | 0005654 | cellular_component | nucleoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
D | 0006508 | biological_process | proteolysis |
D | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
D | 0008104 | biological_process | protein localization |
D | 0009653 | biological_process | anatomical structure morphogenesis |
D | 0016567 | biological_process | protein ubiquitination |
D | 0019941 | biological_process | modification-dependent protein catabolic process |
D | 0030162 | biological_process | regulation of proteolysis |
D | 0031386 | molecular_function | protein tag activity |
D | 0031625 | molecular_function | ubiquitin protein ligase binding |
D | 0036211 | biological_process | protein modification process |
D | 0045116 | biological_process | protein neddylation |
D | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 301 |
Chain | Residue |
A | LEU57 |
A | ASN60 |
A | VAL61 |
A | SER108 |
A | SER109 |
A | ARG111 |
A | HOH510 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 302 |
Chain | Residue |
A | ILE235 |
A | ASP236 |
A | HIS239 |
A | ILE240 |
A | HIS226 |
A | GLY229 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 301 |
Chain | Residue |
C | THR225 |
C | HIS226 |
C | ILE235 |
C | ASP236 |
C | HIS239 |
C | ILE240 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 302 |
Chain | Residue |
C | LEU57 |
C | ASN60 |
C | VAL61 |
C | SER108 |
C | ARG111 |
C | HOH530 |
Functional Information from PROSITE/UniProt
site_id | PS00299 |
Number of Residues | 26 |
Details | UBIQUITIN_1 Ubiquitin domain signature. KerVeEkegIPpqqQrLIYsGkqmnD |
Chain | Residue | Details |
B | LYS27-ASP52 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:19308257, ECO:0000305|PubMed:22691497 |
Chain | Residue | Details |
A | ALA117 | |
C | ALA117 | |
D | LEU8 | |
D | ILE44 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q63KH5 |
Chain | Residue | Details |
A | HIS173 | |
A | GLN193 | |
C | HIS173 | |
C | GLN193 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P29595 |
Chain | Residue | Details |
B | LYS48 | |
D | LYS48 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) |
Chain | Residue | Details |
B | GLY76 | |
D | GLY76 |