5AXI
Crystal structure of Cbl-b TKB domain in complex with Cblin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001784 | molecular_function | phosphotyrosine residue binding |
A | 0004842 | molecular_function | ubiquitin-protein transferase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0007166 | biological_process | cell surface receptor signaling pathway |
A | 0023051 | biological_process | regulation of signaling |
B | 0001784 | molecular_function | phosphotyrosine residue binding |
B | 0004842 | molecular_function | ubiquitin-protein transferase activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0007166 | biological_process | cell surface receptor signaling pathway |
B | 0023051 | biological_process | regulation of signaling |
C | 0001784 | molecular_function | phosphotyrosine residue binding |
C | 0004842 | molecular_function | ubiquitin-protein transferase activity |
C | 0005509 | molecular_function | calcium ion binding |
C | 0007166 | biological_process | cell surface receptor signaling pathway |
C | 0023051 | biological_process | regulation of signaling |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue CA A 401 |
Chain | Residue |
A | ASP221 |
A | THR223 |
A | ASN225 |
A | TYR227 |
A | GLU232 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue CL A 402 |
Chain | Residue |
A | ARG183 |
B | ARG183 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue CL A 403 |
Chain | Residue |
A | TRP243 |
A | LYS175 |
A | PRO242 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue CL A 404 |
Chain | Residue |
A | LYS189 |
A | THR190 |
A | ILE191 |
A | HOH564 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue CA B 401 |
Chain | Residue |
B | ASP221 |
B | THR223 |
B | ASN225 |
B | TYR227 |
B | GLU232 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue CL B 402 |
Chain | Residue |
B | LYS175 |
B | PRO242 |
B | TRP243 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue CA C 401 |
Chain | Residue |
C | ASP221 |
C | THR223 |
C | ASN225 |
C | TYR227 |
C | GLU232 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for Di-peptide GLY E 2 and PTR E 3 |
Chain | Residue |
B | TYR266 |
B | ARG286 |
B | SER288 |
B | CYS289 |
B | THR290 |
B | GLN308 |
E | ASP1 |
E | MET4 |
E | HOH101 |
E | HOH103 |
site_id | AC9 |
Number of Residues | 11 |
Details | binding site for Di-peptide PTR E 3 and MET E 4 |
Chain | Residue |
B | TYR266 |
B | ARG286 |
B | SER288 |
B | CYS289 |
B | THR290 |
B | GLN308 |
B | THR309 |
E | GLY2 |
E | PRO5 |
E | HOH101 |
E | HOH103 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by INSR => ECO:0000250|UniProtKB:P35570 |
Chain | Residue | Details |
E | PTR3 | |
B | GLU232 | |
C | ASP221 | |
C | THR223 | |
C | ASN225 | |
C | TYR227 | |
C | GLU232 | |
A | THR223 | |
A | ASN225 | |
A | TYR227 | |
A | GLU232 | |
B | ASP221 | |
B | THR223 | |
B | ASN225 | |
B | TYR227 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG286 | |
B | ARG286 | |
C | ARG286 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine; by PKC/PRKCQ => ECO:0000250|UniProtKB:Q13191 |
Chain | Residue | Details |
A | SER282 | |
B | SER282 | |
C | SER282 |