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 |