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4A4B

Structure of modified phosphoTyr371-c-Cbl-UbcH5B-ZAP-70 complex

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
C0000166molecular_functionnucleotide binding
C0000209biological_processprotein polyubiquitination
C0004842molecular_functionubiquitin-protein transferase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005829cellular_componentcytosol
C0006511biological_processubiquitin-dependent protein catabolic process
C0016567biological_processprotein ubiquitination
C0016740molecular_functiontransferase activity
C0032991cellular_componentprotein-containing complex
C0036211biological_processprotein modification process
C0051865biological_processprotein autoubiquitination
C0061630molecular_functionubiquitin protein ligase activity
C0061631molecular_functionubiquitin conjugating enzyme activity
C0070062cellular_componentextracellular exosome
C0070936biological_processprotein K48-linked ubiquitination
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 Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1438
ChainResidue
ATHR231
AASN233
ATYR235
AGLU240
AASP229

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL
ChainResidueDetails
CTYR74-LEU89

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 Residues39
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues72
DetailsRegion: {"description":"EF-hand-like"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues102
DetailsRegion: {"description":"SH2-like"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1B47","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CBL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by INSR","evidences":[{"source":"PubMed","id":"11997497","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15144186","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"8943331","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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