Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2Y1M

Structure of native c-Cbl

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 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	4
Details	BINDING SITE FOR RESIDUE ZN B 1436

Chain	Residue
B	CYS384
B	CYS401
B	CYS404
B	CYS381

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1437

Chain	Residue
B	CYS396
B	HIS398
B	CYS416
B	CYS419

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 1436

Chain	Residue
C	CYS381
C	CYS384
C	CYS401
C	CYS404

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 1437

Chain	Residue
C	CYS396
C	HIS398
C	CYS416
C	CYS419

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 1436

Chain	Residue
D	CYS381
D	CYS384
D	CYS401
D	CYS404

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 1437

Chain	Residue
D	CYS396
D	HIS398
D	CYS416
D	CYS419

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN E 1436

Chain	Residue
E	CYS381
E	ILE383
E	CYS384
E	CYS401
E	CYS404

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 1437

Chain	Residue
E	CYS396
E	HIS398
E	CYS416
E	CYS419

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 1436

Chain	Residue
F	CYS381
F	CYS384
F	CYS401
F	CYS404

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 1437

Chain	Residue
F	CYS396
F	HIS398
F	CYS416
F	CYS419

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 1438

Chain	Residue
B	ASP229
B	THR231
B	ASN233
B	TYR235
B	GLU240
B	HOH2008

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 1438

Chain	Residue
D	ASP229
D	THR231
D	ASN233
D	TYR235
D	GLU240

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 1438

Chain	Residue
A	ASP229
A	THR231
A	ASN233
A	TYR235
A	GLU240

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 1438

Chain	Residue
C	ASP229
C	THR231
C	ASN233
C	TYR235
C	GLU240

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 1438

Chain	Residue
E	ASP229
E	THR231
E	ASN233
E	TYR235
E	GLU240

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA F 1438

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	TYR371
B	TYR371
C	TYR371
D	TYR371
E	TYR371
F	TYR371

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)