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2LDR

Solution structure of Helix-RING domain of Cbl-b in the Tyr363 phosphorylated form

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0023051biological_processregulation of signaling
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1373
ChainResidue
ACYS373
ACYS376
AASN379
ACYS393
ACYS396

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1388
ChainResidue
ACYS411
ACYS388
AHIS390
ACYS408
APHE410

Functional Information from PROSITE/UniProt
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CgHlMCtsCL
ChainResidueDetails
ACYS388-LEU397

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues39
DetailsZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
ChainResidueDetails
ACYS373-ARG412

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000305|PubMed:20525694
ChainResidueDetails
APTR363

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PDB entries from 2024-11-06

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