3SLA
X-ray structure of first four repeats of human beta-catenin
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 | 0007155 | biological_process | cell adhesion |
C | 0045296 | molecular_function | cadherin binding |
D | 0007155 | biological_process | cell adhesion |
D | 0045296 | molecular_function | cadherin binding |
E | 0007155 | biological_process | cell adhesion |
E | 0045296 | molecular_function | cadherin binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE GOL A 1 |
Chain | Residue |
A | LYS181 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 2 |
Chain | Residue |
A | LYS242 |
A | SER246 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 4 |
Chain | Residue |
A | VAL173 |
A | GLN177 |
E | ALA272 |
E | LEU275 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 7 |
Chain | Residue |
A | LYS270 |
A | MET271 |
A | ARG274 |
D | ALA152 |
D | GLU155 |
A | GLY268 |
A | ALA269 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL D 3 |
Chain | Residue |
D | THR205 |
D | ASN206 |
D | LYS242 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL D 5 |
Chain | Residue |
A | LEU229 |
A | GLU267 |
D | ASP162 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL E 6 |
Chain | Residue |
E | PRO247 |
E | ASP249 |
E | THR289 |
E | ASN290 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL E 8 |
Chain | Residue |
E | MET189 |
E | GLU226 |
E | LEU229 |
E | LYS233 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA E 1 |
Chain | Residue |
E | HIS223 |
E | ASN261 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA E 2 |
Chain | Residue |
E | THR257 |
E | HIS260 |
E | ASN261 |
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 | 205 |
Details | Repeat: {"description":"ARM 2"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 205 |
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 | 2 |
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 | 5 |
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 | 5 |
Details | Modified residue: {"description":"Phosphoserine; by CDK5","evidences":[{"source":"PubMed","id":"17009320","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |