Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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 Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15144186
ChainResidueDetails
BSER4
DSER4

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8943331, ECO:0007744|PubMed:19690332
ChainResidueDetails
BPTR7
CGLU240
DPTR7
AASN233
ATYR235
AGLU240
CASP229
CTHR231
CASN233
CTYR235

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG294
CARG294

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by INSR => ECO:0000269|PubMed:11997497
ChainResidueDetails
APTR371
CPTR371

217705

PDB entries from 2024-03-27

PDB statisticsPDBj update infoContact PDBjnumon