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5O76

Structure of phosphoY371 c-CBL in complex with ZAP70-peptide and UbV.pCBL ubiquitin variant

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
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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 501
ChainResidue
ACYS381
ACYS384
ACYS401
ACYS404

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 502
ChainResidue
ACYS396
AHIS398
ACYS416
ACYS419

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 503
ChainResidue
ATHR231
AASN233
ATYR235
AGLU240
AHOH613
AASP229

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN C 501
ChainResidue
CCYS381
CCYS384
CCYS401
CCYS404

site_idAC5
Number of Residues3
Detailsbinding site for residue ZN C 502
ChainResidue
CCYS396
CHIS398
CCYS416

site_idAC6
Number of Residues6
Detailsbinding site for residue CA C 503
ChainResidue
CASP229
CTHR231
CASN233
CTYR235
CGLU240
CHOH602

site_idAC7
Number of Residues8
Detailsbinding site for Di-peptide GLY D 6 and PTR D 7
ChainResidue
CTYR274
CARG294
CSER296
CCYS297
CTHR298
CGLN316
DASP5
DTHR8

site_idAC8
Number of Residues11
Detailsbinding site for Di-peptide PTR D 7 and THR D 8
ChainResidue
CTYR274
CARG294
CSER296
CCYS297
CTHR298
CLEU315
CGLN316
CTHR317
DASP5
DGLY6
DPRO9

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFvGkqleD
ChainResidueDetails
ELYS27-ASP52

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 Residues78
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues144
DetailsRegion: {"description":"EF-hand-like"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues204
DetailsRegion: {"description":"SH2-like"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1B47","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CBL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by INSR","evidences":[{"source":"PubMed","id":"11997497","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"8943331","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15144186","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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