5J3X
Structure of c-CBL Y371F
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 |
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 |
B | 0046872 | molecular_function | metal ion binding |
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 |
C | 0046872 | molecular_function | metal ion binding |
D | 0001784 | molecular_function | phosphotyrosine residue binding |
D | 0004842 | molecular_function | ubiquitin-protein transferase activity |
D | 0005509 | molecular_function | calcium ion binding |
D | 0007166 | biological_process | cell surface receptor signaling pathway |
D | 0023051 | biological_process | regulation of signaling |
D | 0046872 | molecular_function | metal ion binding |
E | 0001784 | molecular_function | phosphotyrosine residue binding |
E | 0004842 | molecular_function | ubiquitin-protein transferase activity |
E | 0005509 | molecular_function | calcium ion binding |
E | 0007166 | biological_process | cell surface receptor signaling pathway |
E | 0023051 | biological_process | regulation of signaling |
E | 0046872 | molecular_function | metal ion binding |
F | 0001784 | molecular_function | phosphotyrosine residue binding |
F | 0004842 | molecular_function | ubiquitin-protein transferase activity |
F | 0005509 | molecular_function | calcium ion binding |
F | 0007166 | biological_process | cell surface receptor signaling pathway |
F | 0023051 | biological_process | regulation of signaling |
F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 501 |
Chain | Residue |
A | CYS381 |
A | CYS384 |
A | CYS401 |
A | CYS404 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 502 |
Chain | Residue |
A | CYS396 |
A | HIS398 |
A | CYS416 |
A | CYS419 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CA A 503 |
Chain | Residue |
A | THR231 |
A | ASN233 |
A | TYR235 |
A | GLU240 |
A | ASP229 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN B 501 |
Chain | Residue |
B | CYS381 |
B | CYS384 |
B | CYS401 |
B | CYS404 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN B 502 |
Chain | Residue |
B | CYS396 |
B | HIS398 |
B | CYS416 |
B | CYS419 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CA B 503 |
Chain | Residue |
B | ASP229 |
B | THR231 |
B | ASN233 |
B | TYR235 |
B | GLU240 |
B | HOH608 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN C 501 |
Chain | Residue |
C | CYS381 |
C | CYS384 |
C | CYS401 |
C | CYS404 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue ZN C 502 |
Chain | Residue |
C | CYS396 |
C | HIS398 |
C | CYS416 |
C | CYS419 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue CA C 503 |
Chain | Residue |
C | ASP229 |
C | THR231 |
C | ASN233 |
C | TYR235 |
C | GLU240 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue ZN D 501 |
Chain | Residue |
D | CYS381 |
D | CYS384 |
D | CYS401 |
D | CYS404 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue ZN D 502 |
Chain | Residue |
D | CYS396 |
D | HIS398 |
D | CYS416 |
D | CYS419 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue CA D 503 |
Chain | Residue |
D | ASP229 |
D | THR231 |
D | ASN233 |
D | TYR235 |
D | GLU240 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue ZN E 501 |
Chain | Residue |
E | CYS381 |
E | CYS384 |
E | CYS401 |
E | CYS404 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue ZN E 502 |
Chain | Residue |
E | CYS396 |
E | HIS398 |
E | CYS416 |
E | CYS419 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue CA E 503 |
Chain | Residue |
E | ASP229 |
E | THR231 |
E | ASN233 |
E | TYR235 |
E | GLU240 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue ZN F 501 |
Chain | Residue |
F | CYS381 |
F | CYS384 |
F | CYS401 |
F | CYS404 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue ZN F 502 |
Chain | Residue |
F | CYS396 |
F | HIS398 |
F | CYS416 |
F | CYS419 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue CA F 503 |
Chain | Residue |
F | ASP229 |
F | THR231 |
F | ASN233 |
F | TYR235 |
F | GLU240 |
Functional Information from PROSITE/UniProt
site_id | PS00518 |
Number of Residues | 10 |
Details | ZF_RING_1 Zinc finger RING-type signature. CgHlMCtsCL |
Chain | Residue | Details |
A | CYS396-LEU405 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 234 |
Details | ZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175 |
Chain | Residue | Details |
A | CYS381-ARG420 | |
B | CYS381-ARG420 | |
C | CYS381-ARG420 | |
D | CYS381-ARG420 | |
E | CYS381-ARG420 | |
F | CYS381-ARG420 |
site_id | SWS_FT_FI2 |
Number of Residues | 30 |
Details | BINDING: BINDING => ECO:0007744|PDB:1B47, ECO:0007744|PDB:2CBL |
Chain | Residue | Details |
A | ASP229 | |
B | GLU240 | |
C | ASP229 | |
C | THR231 | |
C | ASN233 | |
C | TYR235 | |
C | GLU240 | |
D | ASP229 | |
D | THR231 | |
D | ASN233 | |
D | TYR235 | |
A | THR231 | |
D | GLU240 | |
E | ASP229 | |
E | THR231 | |
E | ASN233 | |
E | TYR235 | |
E | GLU240 | |
F | ASP229 | |
F | THR231 | |
F | ASN233 | |
F | TYR235 | |
A | ASN233 | |
F | GLU240 | |
A | TYR235 | |
A | GLU240 | |
B | ASP229 | |
B | THR231 | |
B | ASN233 | |
B | TYR235 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG294 | |
B | ARG294 | |
C | ARG294 | |
D | ARG294 | |
E | ARG294 | |
F | ARG294 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: Phosphotyrosine; by INSR => ECO:0000269|PubMed:11997497 |
Chain | Residue | Details |
A | PHE371 | |
B | PHE371 | |
C | PHE371 | |
D | PHE371 | |
E | PHE371 | |
F | PHE371 |