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3VRQ

Crystal structure of the tyrosine kinase binding domain of Cbl-c (PL mutant)

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
B0001784molecular_functionphosphotyrosine residue binding
B0004842molecular_functionubiquitin-protein transferase activity
B0005509molecular_functioncalcium ion binding
B0007166biological_processcell surface receptor signaling pathway
B0023051biological_processregulation of signaling
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP199
ATHR201
ASER203
AHIS205
AGLU210

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BGLU210
BHOH507
BASP199
BTHR201
BSER203
BHIS205

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P22681
ChainResidueDetails
AASP199
ATHR201
AGLU210
BASP199
BTHR201
BGLU210

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AARG264
BARG264

222415

PDB entries from 2024-07-10

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