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2Y1M

Structure of native c-Cbl

Functional Information from GO Data
ChainGOidnamespacecontents
A0001784molecular_functionphosphotyrosine residue binding
A0004842molecular_functionubiquitin-protein transferase activity
A0005509molecular_functioncalcium ion binding
A0007166biological_processcell surface receptor signaling pathway
A0023051biological_processregulation of signaling
A0046872molecular_functionmetal ion binding
B0001784molecular_functionphosphotyrosine residue binding
B0004842molecular_functionubiquitin-protein transferase activity
B0005509molecular_functioncalcium ion binding
B0007166biological_processcell surface receptor signaling pathway
B0023051biological_processregulation of signaling
B0046872molecular_functionmetal ion binding
C0001784molecular_functionphosphotyrosine residue binding
C0004842molecular_functionubiquitin-protein transferase activity
C0005509molecular_functioncalcium ion binding
C0007166biological_processcell surface receptor signaling pathway
C0023051biological_processregulation of signaling
C0046872molecular_functionmetal ion binding
D0001784molecular_functionphosphotyrosine residue binding
D0004842molecular_functionubiquitin-protein transferase activity
D0005509molecular_functioncalcium ion binding
D0007166biological_processcell surface receptor signaling pathway
D0023051biological_processregulation of signaling
D0046872molecular_functionmetal ion binding
E0001784molecular_functionphosphotyrosine residue binding
E0004842molecular_functionubiquitin-protein transferase activity
E0005509molecular_functioncalcium ion binding
E0007166biological_processcell surface receptor signaling pathway
E0023051biological_processregulation of signaling
E0046872molecular_functionmetal ion binding
F0001784molecular_functionphosphotyrosine residue binding
F0004842molecular_functionubiquitin-protein transferase activity
F0005509molecular_functioncalcium ion binding
F0007166biological_processcell surface receptor signaling pathway
F0023051biological_processregulation of signaling
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1436
ChainResidue
ACYS381
ACYS384
ACYS401
ACYS404

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1437
ChainResidue
ACYS396
AHIS398
ACYS416
ACYS419

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1436
ChainResidue
BCYS384
BCYS401
BCYS404
BCYS381

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1437
ChainResidue
BCYS396
BHIS398
BCYS416
BCYS419

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1436
ChainResidue
CCYS381
CCYS384
CCYS401
CCYS404

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1437
ChainResidue
CCYS396
CHIS398
CCYS416
CCYS419

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1436
ChainResidue
DCYS381
DCYS384
DCYS401
DCYS404

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1437
ChainResidue
DCYS396
DHIS398
DCYS416
DCYS419

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN E 1436
ChainResidue
ECYS381
EILE383
ECYS384
ECYS401
ECYS404

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 1437
ChainResidue
ECYS396
EHIS398
ECYS416
ECYS419

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 1436
ChainResidue
FCYS381
FCYS384
FCYS401
FCYS404

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 1437
ChainResidue
FCYS396
FHIS398
FCYS416
FCYS419

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1438
ChainResidue
BASP229
BTHR231
BASN233
BTYR235
BGLU240
BHOH2008

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA D 1438
ChainResidue
DASP229
DTHR231
DASN233
DTYR235
DGLU240

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1438
ChainResidue
AASP229
ATHR231
AASN233
ATYR235
AGLU240

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 1438
ChainResidue
CASP229
CTHR231
CASN233
CTYR235
CGLU240

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA E 1438
ChainResidue
EASP229
ETHR231
EASN233
ETYR235
EGLU240

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA F 1438
ChainResidue
FASP229
FTHR231
FASN233
FTYR235
FGLU240

Functional Information from PROSITE/UniProt
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CgHlMCtsCL
ChainResidueDetails
ACYS396-LEU405

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1824
DetailsDomain: {"description":"Cbl-PTB","evidences":[{"source":"PROSITE-ProRule","id":"PRU00839","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues234
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues768
DetailsRegion: {"description":"4H"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues432
DetailsRegion: {"description":"EF-hand-like"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues612
DetailsRegion: {"description":"SH2-like"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1B47","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CBL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine; by INSR","evidences":[{"source":"PubMed","id":"11997497","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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