4A4B
Structure of modified phosphoTyr371-c-Cbl-UbcH5B-ZAP-70 complex
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 |
A | 0046872 | molecular_function | metal ion binding |
C | 0000209 | biological_process | protein polyubiquitination |
C | 0004842 | molecular_function | ubiquitin-protein transferase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005634 | cellular_component | nucleus |
C | 0005654 | cellular_component | nucleoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
C | 0016567 | biological_process | protein ubiquitination |
C | 0016740 | molecular_function | transferase activity |
C | 0019787 | molecular_function | ubiquitin-like protein transferase activity |
C | 0032991 | cellular_component | protein-containing complex |
C | 0036211 | biological_process | protein modification process |
C | 0051865 | biological_process | protein autoubiquitination |
C | 0061630 | molecular_function | ubiquitin protein ligase activity |
C | 0061631 | molecular_function | ubiquitin conjugating enzyme activity |
C | 0070062 | cellular_component | extracellular exosome |
C | 0070936 | biological_process | protein K48-linked ubiquitination |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1436 |
Chain | Residue |
A | CYS381 |
A | CYS384 |
A | CYS401 |
A | CYS404 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1437 |
Chain | Residue |
A | CYS396 |
A | HIS398 |
A | CYS416 |
A | CYS419 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 1438 |
Chain | Residue |
A | THR231 |
A | ASN233 |
A | TYR235 |
A | GLU240 |
A | ASP229 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133 |
Chain | Residue | Details |
C | CYS85 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
B | PTR7 | |
A | THR231 | |
A | ASN233 | |
A | TYR235 | |
A | GLU240 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG294 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by INSR => ECO:0000269|PubMed:11997497 |
Chain | Residue | Details |
A | PTR371 |