7Z36
Crystal structure of the KAP1 tripartite motif in complex with the ZNF93 KRAB domain
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003796 | molecular_function | lysozyme activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009253 | biological_process | peptidoglycan catabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0016998 | biological_process | cell wall macromolecule catabolic process |
A | 0030430 | cellular_component | host cell cytoplasm |
A | 0031640 | biological_process | killing of cells of another organism |
A | 0042742 | biological_process | defense response to bacterium |
A | 0044659 | biological_process | viral release from host cell by cytolysis |
B | 0003796 | molecular_function | lysozyme activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0009253 | biological_process | peptidoglycan catabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0016998 | biological_process | cell wall macromolecule catabolic process |
B | 0030430 | cellular_component | host cell cytoplasm |
B | 0031640 | biological_process | killing of cells of another organism |
B | 0042742 | biological_process | defense response to bacterium |
B | 0044659 | biological_process | viral release from host cell by cytolysis |
C | 0043130 | molecular_function | ubiquitin binding |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
S | 0043130 | molecular_function | ubiquitin binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | SER2 | |
S | SER2 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | ASP44 | |
B | ASP44 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | LEU56 | |
A | PHE128 | |
B | LEU56 | |
B | PHE128 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
Chain | Residue | Details |
A | SER141 | |
A | ASN156 | |
B | SER141 | |
B | ASN156 |
site_id | SWS_FT_FI5 |
Number of Residues | 112 |
Details | ZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175 |
Chain | Residue | Details |
A | CYS196-LYS252 | |
B | CYS196-LYS252 |
site_id | SWS_FT_FI6 |
Number of Residues | 94 |
Details | ZN_FING: B box-type 1; atypical => ECO:0000255|PROSITE-ProRule:PRU00024 |
Chain | Residue | Details |
A | ASN279-ALA326 | |
B | ASN279-ALA326 |
site_id | SWS_FT_FI7 |
Number of Residues | 82 |
Details | ZN_FING: B box-type 2 => ECO:0000255|PROSITE-ProRule:PRU00024 |
Chain | Residue | Details |
A | LYS335-ASN376 | |
B | LYS335-ASN376 |
site_id | SWS_FT_FI8 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00024 |
Chain | Residue | Details |
A | GLU284 | |
B | VAL287 | |
B | ASP308 | |
B | GLN312 | |
B | GLN340 | |
B | THR343 | |
B | ASP363 | |
B | ILE368 | |
A | VAL287 | |
A | ASP308 | |
A | GLN312 | |
A | GLN340 | |
A | THR343 | |
A | ASP363 | |
A | ILE368 | |
B | GLU284 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER269 | |
B | SER269 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q62318 |
Chain | Residue | Details |
A | LEU397 | |
B | LEU397 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS435 | |
B | LYS435 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | ALA471 | |
B | ALA471 |
site_id | SWS_FT_FI13 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS258 | |
A | THR403 | |
B | LYS258 | |
B | THR403 |
site_id | SWS_FT_FI14 |
Number of Residues | 8 |
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 | LYS330 | |
A | ASP385 | |
A | GLY392 | |
A | ASP450 | |
B | LYS330 | |
B | ASP385 | |
B | GLY392 | |
B | ASP450 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS435 | |
B | LYS435 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447 |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
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 |