3SL9
X-ray structure of Beta catenin in complex with Bcl9
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0007155 | biological_process | cell adhesion |
| A | 0045296 | molecular_function | cadherin binding |
| B | 0007155 | biological_process | cell adhesion |
| B | 0045296 | molecular_function | cadherin binding |
| C | 0003713 | molecular_function | transcription coactivator activity |
| C | 0008013 | molecular_function | beta-catenin binding |
| C | 0060070 | biological_process | canonical Wnt signaling pathway |
| D | 0003713 | molecular_function | transcription coactivator activity |
| D | 0008013 | molecular_function | beta-catenin binding |
| D | 0060070 | biological_process | canonical Wnt signaling pathway |
| E | 0007155 | biological_process | cell adhesion |
| E | 0045296 | molecular_function | cadherin binding |
| F | 0003713 | molecular_function | transcription coactivator activity |
| F | 0008013 | molecular_function | beta-catenin binding |
| F | 0060070 | biological_process | canonical Wnt signaling pathway |
| G | 0007155 | biological_process | cell adhesion |
| G | 0045296 | molecular_function | cadherin binding |
| H | 0003713 | molecular_function | transcription coactivator activity |
| H | 0008013 | molecular_function | beta-catenin binding |
| H | 0060070 | biological_process | canonical Wnt signaling pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 1 |
| Chain | Residue |
| A | ASP299 |
| A | GLN302 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 2 |
| Chain | Residue |
| A | GLU163 |
| A | GLN165 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 306 |
| Chain | Residue |
| E | LYS288 |
| A | ASP249 |
| A | LYS288 |
| A | THR289 |
| A | ASN290 |
| A | PHE293 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IMD A 307 |
| Chain | Residue |
| A | THR205 |
| A | SER246 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 3 |
| Chain | Residue |
| C | LEU351 |
| C | GLN353 |
| E | MET243 |
| E | SER246 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 5 |
| Chain | Residue |
| A | HOH87 |
| A | ARG274 |
| B | GLN280 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG C 2 |
| Chain | Residue |
| C | HOH49 |
| C | HOH51 |
| C | GLU357 |
| E | ALA276 |
| E | GLY277 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL B 308 |
| Chain | Residue |
| B | ASP299 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 309 |
| Chain | Residue |
| B | SER222 |
| B | HIS223 |
| B | HIS265 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 4 |
| Chain | Residue |
| B | HIS176 |
| B | LYS180 |
| B | ASN220 |
| B | TYR254 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 7 |
| Chain | Residue |
| B | PHE253 |
| B | LYS292 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 6 |
| Chain | Residue |
| B | HOH89 |
| B | LEU263 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 3 |
| Chain | Residue |
| A | MET271 |
| B | HOH78 |
| B | LYS281 |
| B | LEU285 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 306 |
| Chain | Residue |
| B | HOH58 |
| B | THR205 |
| B | ASN206 |
| B | LYS242 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IMD B 307 |
| Chain | Residue |
| A | PRO238 |
| B | GLN203 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO E 8 |
| Chain | Residue |
| E | HOH93 |
| E | GLY235 |
| E | PRO238 |
| E | ALA272 |
| F | GOL4 |
| site_id | BC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL E 2 |
| Chain | Residue |
| E | ASP299 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO E 9 |
| Chain | Residue |
| C | GLU360 |
| E | GLY245 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO E 10 |
| Chain | Residue |
| E | LYS292 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO E 11 |
| Chain | Residue |
| E | PHE232 |
| E | GLU267 |
| E | GLY268 |
| F | GLN364 |
| F | ASP368 |
| F | ARG371 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG E 5 |
| Chain | Residue |
| E | HOH125 |
| E | ARG151 |
| E | ARG274 |
| E | GLN280 |
| G | ALA305 |
| site_id | CC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IMD E 4 |
| Chain | Residue |
| E | LYS158 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL F 4 |
| Chain | Residue |
| E | EDO8 |
| E | ALA272 |
| E | ALA276 |
| F | MET372 |
| site_id | CC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL G 1 |
| Chain | Residue |
| A | HIS260 |
| G | HOH316 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IMD G 5 |
| Chain | Residue |
| A | HOH17 |
| G | HIS260 |
| site_id | CC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IMD G 7 |
| Chain | Residue |
| G | ASP299 |
| G | GLN302 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 160 |
| Details | Repeat: {"description":"ARM 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 164 |
| Details | Repeat: {"description":"ARM 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 164 |
| Details | Repeat: {"description":"ARM 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 88 |
| Details | Region: {"description":"Interaction with BCL9","evidences":[{"source":"PubMed","id":"17052462","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphotyrosine; by FYN and PTK6","evidences":[{"source":"PubMed","id":"12640114","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20026641","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by CDK5","evidences":[{"source":"PubMed","id":"17009320","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by CDK5","evidences":[{"source":"PubMed","id":"17009320","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 48 |
| Details | Region: {"description":"Interaction with CTNNB1","evidences":[{"source":"PubMed","id":"17052462","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9D219","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






