4KC9
Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000151 | cellular_component | ubiquitin ligase complex |
| A | 0000209 | biological_process | protein polyubiquitination |
| A | 0004842 | molecular_function | ubiquitin-protein transferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015030 | cellular_component | Cajal body |
| A | 0016567 | biological_process | protein ubiquitination |
| A | 0016604 | cellular_component | nuclear body |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019005 | cellular_component | SCF ubiquitin ligase complex |
| A | 0019787 | molecular_function | ubiquitin-like protein transferase activity |
| A | 0031462 | cellular_component | Cul2-RING ubiquitin ligase complex |
| A | 0031463 | cellular_component | Cul3-RING ubiquitin ligase complex |
| A | 0031464 | cellular_component | Cul4A-RING E3 ubiquitin ligase complex |
| A | 0031624 | molecular_function | ubiquitin conjugating enzyme binding |
| A | 0031625 | molecular_function | ubiquitin protein ligase binding |
| A | 0039585 | biological_process | PKR/eIFalpha signaling |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061630 | molecular_function | ubiquitin protein ligase activity |
| A | 0097413 | cellular_component | Lewy body |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 601 |
| Chain | Residue |
| A | CYS344 |
| A | CYS347 |
| A | CYS362 |
| A | CYS367 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 602 |
| Chain | Residue |
| A | CYS372 |
| A | CYS375 |
| A | HIS382 |
| A | CYS389 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 603 |
| Chain | Residue |
| A | CYS281 |
| A | CYS297 |
| A | CYS299 |
| A | CYS276 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 604 |
| Chain | Residue |
| A | CYS304 |
| A | CYS307 |
| A | HIS312 |
| A | CYS317 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 605 |
| Chain | Residue |
| A | GLN108 |
| A | CYS186 |
| A | CYS189 |
| A | CYS208 |
| A | CYS211 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 606 |
| Chain | Residue |
| A | CYS203 |
| A | HIS205 |
| A | CYS231 |
| A | CYS236 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 50 |
| Details | ZN_FING: RING-type 1 => ECO:0000255|PROSITE-ProRule:PRU01221 |
| Chain | Residue | Details |
| A | CYS186-CYS236 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 61 |
| Details | ZN_FING: IBR-type => ECO:0000255|PROSITE-ProRule:PRU01221 |
| Chain | Residue | Details |
| A | LEU256-CYS317 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 31 |
| Details | ZN_FING: RING-type 2; atypical => ECO:0000255|PROSITE-ProRule:PRU01221 |
| Chain | Residue | Details |
| A | CYS344-CYS375 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:23707686 |
| Chain | Residue | Details |
| A | CYS357 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23707686, ECO:0007744|PDB:4KBL, ECO:0007744|PDB:4KC9 |
| Chain | Residue | Details |
| A | CYS208 | |
| A | CYS211 | |
| A | CYS231 | |
| A | CYS236 | |
| A | CYS276 | |
| A | CYS281 | |
| A | CYS297 | |
| A | CYS299 | |
| A | CYS304 | |
| A | CYS307 | |
| A | HIS312 | |
| A | CYS317 | |
| A | CYS186 | |
| A | CYS189 | |
| A | CYS203 | |
| A | HIS205 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:15236971, ECO:0000269|PubMed:23707686, ECO:0000269|PubMed:24058416, ECO:0007744|PDB:1WD2, ECO:0007744|PDB:2M9Y, ECO:0007744|PDB:4KBL, ECO:0007744|PDB:4KC9 |
| Chain | Residue | Details |
| A | CYS367 | |
| A | CYS344 | |
| A | CYS347 | |
| A | CYS362 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23707686, ECO:0000269|PubMed:24058416, ECO:0007744|PDB:2M9Y, ECO:0007744|PDB:4KBL, ECO:0007744|PDB:4KC9 |
| Chain | Residue | Details |
| A | CYS375 | |
| A | HIS382 | |
| A | CYS389 | |
| A | CYS372 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z1K5 |
| Chain | Residue | Details |
| A | LYS142 |
