6QU1
Crystal structure of the KAP1 RBCC domain in complex with the SMARCAD1 CUE1 domain at 3.7 angstrom resolution.
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 1001 |
| Chain | Residue |
| A | CYS65 |
| A | GLY66 |
| A | CYS68 |
| A | CYS88 |
| A | CYS91 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 1002 |
| Chain | Residue |
| A | CYS83 |
| A | HIS85 |
| A | CYS117 |
| A | CYS120 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 1003 |
| Chain | Residue |
| A | CYS209 |
| A | HIS212 |
| A | CYS229 |
| A | CYS232 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 1004 |
| Chain | Residue |
| A | CYS221 |
| A | SER223 |
| A | CYS224 |
| A | HIS237 |
| A | HIS240 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| D | SER152 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 47 |
| Details | ZN_FING: B box-type 1; atypical => ECO:0000255|PROSITE-ProRule:PRU00024 |
| Chain | Residue | Details |
| A | TYR208-LEU255 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 41 |
| Details | ZN_FING: B box-type 2 => ECO:0000255|PROSITE-ProRule:PRU00024 |
| Chain | Residue | Details |
| A | GLU204-LEU245 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00024 |
| Chain | Residue | Details |
| A | LYS213 | |
| A | PRO216 | |
| A | HIS237 | |
| A | GLN241 | |
| A | CYS209 | |
| A | HIS212 | |
| A | CYS232 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER198 | |
| A | SER417 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q62318 |
| Chain | Residue | Details |
| A | LYS266 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS304 | |
| A | LYS377 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS340 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS127 | |
| A | LYS272 | |
| A | LYS407 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LEU259 | |
| A | LYS254 | |
| A | LYS261 | |
| A | LYS319 | |
| A | LYS434 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS304 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447 |
| Chain | Residue | Details |
| A | LYS366 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS377 |
